iLID/SspB

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

High ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination, but reduce reversibility.

Conversely, high ligand densities restrict mobility, enabling adhesion asymmetry and GUV migration upon localized illumination but at the cost of reduced reversibility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility and density must be balanced to achieve reversible, light-guided motility.

These results define a design space in which both ligand mobility and density must be finely balanced to achieve reversible, light-guided motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

Ligand mobility is essential for dynamic interactions but can cause ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

We find that ligand mobility, while essential for dynamic interactions, can lead to ligand-receptor clustering that disrupts adhesion asymmetry and limits directional motility.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method is flexible and versatile for regulating protein localization with high spatial and temporal precision using blue light.

Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

The method uses immobilized iLID on supported lipid bilayers and on the outer membrane of giant unilamellar vesicles.

we immobilize the photoswitchable protein iLID (improved light-inducible dimer) on supported lipid bilayers (SLBs) and on the outer membrane of giant unilamellar vesicles (GUVs)

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and recruits Nano-fused proteins of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

Upon local blue light illumination, iLID binds Nano and enables recruitment of a Nano-fused protein of interest from solution to the illuminated membrane area.

Upon local blue light illumination, iLID binds to its partner Nano (wild-type SspB) and allows the recruitment of any protein of interest (POI) fused to Nano from the solution to the illuminated area on the membrane.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

A method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The described method fabricates light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.

a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

The iLID-Nano interaction is reversible in the dark, enabling dynamic binding and release of the recruited protein of interest.

This binding is reversible in the dark, which provides dynamic binding and release of the POI.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

In an endothelial cell monolayer, Opto-RhoGEFs demonstrated precise temporal control of vascular barrier strength through a cell-cell overlap-dependent and VE-cadherin-independent mechanism.

The resulting optogenetically recruitable RhoGEFs (Opto-RhoGEFs) were tested in an endothelial cell monolayer and demonstrated precise temporal control of vascular barrier strength by a cell-cell overlap-dependent, VE-cadherin-independent, mechanism.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Opto-RhoGEFs enabled precise optogenetic control of endothelial cell morphology, including cell size, cell roundness, local extension, and cell contraction.

Furthermore, Opto-RhoGEFs enabled precise optogenetic control in endothelial cells over morphological features such as cell size, cell roundness, local extension, and cell contraction.

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID-based Opto-RhoGEFs allow reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

iLID enables reversible, non-invasive, subcellular activation of Rho GTPase signaling by recruiting a GEF to a specific area at the plasma membrane.

This tool allows for Rho GTPase activation at the subcellular level in a reversible and non-invasive manner by recruiting a GEF to a specific area at the plasma membrane

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

Membrane protrusions at the junction region can rapidly increase endothelial barrier integrity independently of VE-cadherin.

found that membrane protrusions at the junction region can rapidly increase barrier integrity independent of VE-cadherin

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was applied to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for activating Cdc42, Rac, and Rho, respectively.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

GEF domains from ITSN1, TIAM1, and p63RhoGEF were integrated into iLID to create Opto-RhoGEFs for optogenetic control of Rho GTPase signaling.

Guanine-nucleotide exchange factor (GEF) domains from ITSN1, TIAM1, and p63RhoGEF, activating Cdc42, Rac, and Rho, respectively, were integrated into the optogenetic recruitment tool improved light-induced dimer (iLID).

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

The iLID membrane tag was optimized and HaloTag was added to increase flexibility for multiplex imaging.

The membrane tag of iLID was optimized and a HaloTag was applied to gain more flexibility for multiplex imaging.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

OptoPAK1 was designed to function independently of endogenous biochemical regulation in a constitutively active manner with minimal activity in the dark state.

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

The authors developed a genetically expressed, light-responsive optogenetic analog of PAK1 called optoPAK1.

We developed an engineering strategy to construct a genetically expressed, light-responsive optogenetic analog of PAK1 (optoPAK1)

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.

the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

Upon illumination, optoPAK1 migrates to specified intracellular sites.

upon illumination, optoPAK1 migrates to specified intracellular sites

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

iLID and SspB heterodimerize upon blue-light illumination.

It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The improved light-induced dimer system iLid was used to recruit and photoactivate the optoPAK1 protein analog at discrete subcellular domains.

We employed the improved light-induced dimer (iLid) system as a means to recruit and photoactivate the protein analog at discrete subcellular domains.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.

This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

Preliminary data indicated that optoPAK1 phosphorylates the designed intracellular reporters in a light-dependent fashion.

preliminary data displayed that optoPAK1 phosphorylates these reporters in a light-dependent fashion

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.

We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

Using mem-iLID, the authors obtained two pure and fully functional enzymes, a DNA polymerase and a light-activated adenylyl cyclase, quickly.

We demonstrate the quickly obtained yield of two pure and fully functional enzymes: a DNA polymerase and a light-activated adenylyl cyclase.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The findings provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations, including micron-scale regions of the plasma membrane.

These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane.

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

The iLID system enables selective recruitment of components to subcellular locations such as micron-scale regions of the plasma membrane.

the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared with the commonly used C-terminal iLID fusion, large N-terminal anchor fusions provide stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

The study defines guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Consistent recruitment in optogenetic dimerization systems is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

Within iLID-based recruitment, consistent recruitment is limited by heterogeneous optogenetic component expression and spatial precision is reduced by protein diffusion, especially over long time scales.

Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

In mem-iLID, membrane-anchored AsLOV2-SsrA captures cytosolic SspB-POI under light and releases it in the dark after centrifugation and washing.

The SspB-POI can be captured to the membrane fraction through light-induced binding to AsLOV2-SsrA and then released purely to fresh buffer in the dark after simple centrifugation and washing.

Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

Anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics in the iLID system.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics