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.

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.

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)

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.

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 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.

Genetically encoded biosensors and optogenetic tools have been developed to study dynamic T cell signaling pathways in live cells.

Therefore, genetically encoded biosensors and optogenetic tools have been developed to study dynamic T cell signaling pathways in live cells.

The reviewed optical tools have been primarily applied to dynamic molecular events in TCR signaling and may aid understanding of CAR activation and function.

They have been primarily applied to the study of dynamic molecular events in TCR signaling, and they will further aid in understanding the mechanisms of CAR activation and function.

These optical technologies revealed dynamic and complex molecular mechanisms at each stage of T cell signaling pathways.

We review these cutting-edge technologies that revealed dynamic and complex molecular mechanisms at each stage of T cell signaling pathways.

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.

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 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

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 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.

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)

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

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 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

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.

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 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, 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.

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.

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

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

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

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

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

In the iLID system, anchoring strategy affects component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics.

The authors established mem-iLID as an easy and fast purification method for soluble proteins under mild conditions based on iLID.

Here we established an easy and fast purification method for soluble proteins under mild conditions, based on the light-induced protein dimerization system improved light-induced dimer (iLID)

The authors established mem-iLID as an easy and fast purification method for soluble proteins under mild conditions based on iLID.

Here we established an easy and fast purification method for soluble proteins under mild conditions, based on the light-induced protein dimerization system improved light-induced dimer (iLID)

The authors established mem-iLID as an easy and fast purification method for soluble proteins under mild conditions based on iLID.

Here we established an easy and fast purification method for soluble proteins under mild conditions, based on the light-induced protein dimerization system improved light-induced dimer (iLID)

The authors established mem-iLID as an easy and fast purification method for soluble proteins under mild conditions based on iLID.

Here we established an easy and fast purification method for soluble proteins under mild conditions, based on the light-induced protein dimerization system improved light-induced dimer (iLID)

The authors established mem-iLID as an easy and fast purification method for soluble proteins under mild conditions based on iLID.

Here we established an easy and fast purification method for soluble proteins under mild conditions, based on the light-induced protein dimerization system improved light-induced dimer (iLID)

The authors established mem-iLID as an easy and fast purification method for soluble proteins under mild conditions based on iLID.

Here we established an easy and fast purification method for soluble proteins under mild conditions, based on the light-induced protein dimerization system improved light-induced dimer (iLID)

The authors established mem-iLID as an easy and fast purification method for soluble proteins under mild conditions based on iLID.

Here we established an easy and fast purification method for soluble proteins under mild conditions, based on the light-induced protein dimerization system improved light-induced dimer (iLID)

mem-iLID is flexible in scale and economic.

This method, named mem-iLID, is very flexible in scale and economic.

mem-iLID is flexible in scale and economic.

This method, named mem-iLID, is very flexible in scale and economic.

mem-iLID is flexible in scale and economic.

This method, named mem-iLID, is very flexible in scale and economic.

mem-iLID is flexible in scale and economic.

This method, named mem-iLID, is very flexible in scale and economic.

mem-iLID is flexible in scale and economic.

This method, named mem-iLID, is very flexible in scale and economic.

mem-iLID is flexible in scale and economic.

This method, named mem-iLID, is very flexible in scale and economic.

mem-iLID is flexible in scale and economic.

This method, named mem-iLID, is very flexible in scale and economic.

The optogenetic small GTPase control tools were characterized with red fluorescence intensity-based small GTPase biosensors and their specificities were confirmed.

We characterized these optogenetic tools with genetically encoded red fluorescence intensity-based small GTPase biosensors and confirmed these optogenetic tools' specificities.

The optogenetic small GTPase control tools were characterized with red fluorescence intensity-based small GTPase biosensors and their specificities were confirmed.

We characterized these optogenetic tools with genetically encoded red fluorescence intensity-based small GTPase biosensors and confirmed these optogenetic tools' specificities.

The optogenetic small GTPase control tools were characterized with red fluorescence intensity-based small GTPase biosensors and their specificities were confirmed.

We characterized these optogenetic tools with genetically encoded red fluorescence intensity-based small GTPase biosensors and confirmed these optogenetic tools' specificities.

The optogenetic small GTPase control tools were characterized with red fluorescence intensity-based small GTPase biosensors and their specificities were confirmed.

We characterized these optogenetic tools with genetically encoded red fluorescence intensity-based small GTPase biosensors and confirmed these optogenetic tools' specificities.

The optogenetic small GTPase control tools were characterized with red fluorescence intensity-based small GTPase biosensors and their specificities were confirmed.

We characterized these optogenetic tools with genetically encoded red fluorescence intensity-based small GTPase biosensors and confirmed these optogenetic tools' specificities.

The optogenetic small GTPase control tools were characterized with red fluorescence intensity-based small GTPase biosensors and their specificities were confirmed.

We characterized these optogenetic tools with genetically encoded red fluorescence intensity-based small GTPase biosensors and confirmed these optogenetic tools' specificities.

The optogenetic small GTPase control tools were characterized with red fluorescence intensity-based small GTPase biosensors and their specificities were confirmed.

We characterized these optogenetic tools with genetically encoded red fluorescence intensity-based small GTPase biosensors and confirmed these optogenetic tools' specificities.

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID)

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID)

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID)

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID)

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID)

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID)

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID)

The study defines guidelines for component expression regimes that optimize 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 that optimize 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 that optimize 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 that optimize 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 that optimize 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 that optimize 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 that optimize 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 that optimize 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 engineered switch can be used to initiate signaling pathways in a specific region of a cell.

can be used to initiate signaling pathways in a specific region of a cell

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because more colocalization was seen in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The engineered switch has more than 50-fold change in binding affinity upon light stimulation.

has more than 50-fold change in binding affinity upon light stimulation

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V dimer variant displays a 42-fold change in binding affinity upon blue-light activation, from 3 b1 2 bcM to 125 b1 40 bcM.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

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 study defines 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 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 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 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 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 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 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 authors developed and applied methods to identify mutations that improve the effectiveness of a light-induced dimer.

Here, we develop and apply methods for identifying mutations that improve the effectiveness of a light-induced dimer.

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

The iLID-SspB interaction was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM)

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

The N414L point mutation in the LOV domain lengthened the reversion half-life of iLID.

with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB

Anchoring strategy in the iLID system affects component expression and diffusion, which impact recruitment strength, kinetics, and spatial dynamics.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

Anchoring strategy in the iLID system affects component expression and diffusion, which impact recruitment strength, kinetics, and spatial dynamics.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

Anchoring strategy in the iLID system affects component expression and diffusion, which impact recruitment strength, kinetics, and spatial dynamics.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

Anchoring strategy in the iLID system affects component expression and diffusion, which impact recruitment strength, kinetics, and spatial dynamics.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

Anchoring strategy in the iLID system affects component expression and diffusion, which impact recruitment strength, kinetics, and spatial dynamics.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

Anchoring strategy in the iLID system affects component expression and diffusion, which impact recruitment strength, kinetics, and spatial dynamics.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

Anchoring strategy in the iLID system affects component expression and diffusion, which impact recruitment strength, kinetics, and spatial dynamics.

we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics

The engineered switch is modular.

The engineered switch is modular

The engineered switch can be used in most organisms.

can be used in most organisms

This review concerns the construction of light-activated neurotrophin receptors using iLID.

This review concerns the construction of light-activated neurotrophin receptors using iLID.

This review concerns the construction of light-activated neurotrophin receptors using iLID.

This review concerns the construction of light-activated neurotrophin receptors using iLID.

This review concerns the construction of light-activated neurotrophin receptors using iLID.

This review concerns the construction of light-activated neurotrophin receptors using iLID.

This review concerns the construction of light-activated neurotrophin receptors using iLID.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

Thus, we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID).

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

Thus, we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID).

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

Thus, we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID).

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

Thus, we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID).

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

Thus, we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID).

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

Thus, we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID).

The authors constructed optogenetic tools to control the activity of small GTPases using the improved light-inducible dimer system iLID.

Thus, we constructed optogenetic tools to control the activity of small GTPases (RhoA, Rac1, Cdc42, Ras, Rap, and Ral) using an improved light-inducible dimer system (iLID).

opto-iTrkA and opto-iTrkB reproduce downstream ERK and Akt signaling only in the presence of tdnano.

We demonstrate that iLID opto-iTrkA and opto-iTrkB are capable of reproducing downstream ERK and Akt signaling only in the presence of tdnano.

opto-iTrkA and opto-iTrkB reproduce downstream ERK and Akt signaling only in the presence of tdnano.

We demonstrate that iLID opto-iTrkA and opto-iTrkB are capable of reproducing downstream ERK and Akt signaling only in the presence of tdnano.

opto-iTrkA and opto-iTrkB reproduce downstream ERK and Akt signaling only in the presence of tdnano.

We demonstrate that iLID opto-iTrkA and opto-iTrkB are capable of reproducing downstream ERK and Akt signaling only in the presence of tdnano.

opto-iTrkA and opto-iTrkB reproduce downstream ERK and Akt signaling only in the presence of tdnano.

We demonstrate that iLID opto-iTrkA and opto-iTrkB are capable of reproducing downstream ERK and Akt signaling only in the presence of tdnano.

opto-iTrkA and opto-iTrkB reproduce downstream ERK and Akt signaling only in the presence of tdnano.

We demonstrate that iLID opto-iTrkA and opto-iTrkB are capable of reproducing downstream ERK and Akt signaling only in the presence of tdnano.

opto-iTrkA and opto-iTrkB reproduce downstream ERK and Akt signaling only in the presence of tdnano.

We demonstrate that iLID opto-iTrkA and opto-iTrkB are capable of reproducing downstream ERK and Akt signaling only in the presence of tdnano.

opto-iTrkA and opto-iTrkB reproduce downstream ERK and Akt signaling only in the presence of tdnano.

We demonstrate that iLID opto-iTrkA and opto-iTrkB are capable of reproducing downstream ERK and Akt signaling only in the presence of tdnano.

Using iLID to control Rac- or Cdc42-specific GEFs allowed bypass of extracellular signaling events and precise manipulation of localized GTPase activity.

Using iLID, we optogenetically controlled guanine nucleotide exchange factors (GEFs), specific for Rac or Cdc42. This approach allowed us to bypass extracellular signaling events and precisely manipulate localized GTPase activity.

Using iLID to control Rac- or Cdc42-specific GEFs allowed bypass of extracellular signaling events and precise manipulation of localized GTPase activity.

Using iLID, we optogenetically controlled guanine nucleotide exchange factors (GEFs), specific for Rac or Cdc42. This approach allowed us to bypass extracellular signaling events and precisely manipulate localized GTPase activity.

Using iLID to control Rac- or Cdc42-specific GEFs allowed bypass of extracellular signaling events and precise manipulation of localized GTPase activity.

Using iLID, we optogenetically controlled guanine nucleotide exchange factors (GEFs), specific for Rac or Cdc42. This approach allowed us to bypass extracellular signaling events and precisely manipulate localized GTPase activity.

Using iLID to control Rac- or Cdc42-specific GEFs allowed bypass of extracellular signaling events and precise manipulation of localized GTPase activity.

Using iLID, we optogenetically controlled guanine nucleotide exchange factors (GEFs), specific for Rac or Cdc42. This approach allowed us to bypass extracellular signaling events and precisely manipulate localized GTPase activity.

Using iLID to control Rac- or Cdc42-specific GEFs allowed bypass of extracellular signaling events and precise manipulation of localized GTPase activity.

Using iLID, we optogenetically controlled guanine nucleotide exchange factors (GEFs), specific for Rac or Cdc42. This approach allowed us to bypass extracellular signaling events and precisely manipulate localized GTPase activity.

Using iLID to control Rac- or Cdc42-specific GEFs allowed bypass of extracellular signaling events and precise manipulation of localized GTPase activity.

Using iLID, we optogenetically controlled guanine nucleotide exchange factors (GEFs), specific for Rac or Cdc42. This approach allowed us to bypass extracellular signaling events and precisely manipulate localized GTPase activity.

Using iLID to control Rac- or Cdc42-specific GEFs allowed bypass of extracellular signaling events and precise manipulation of localized GTPase activity.

Using iLID, we optogenetically controlled guanine nucleotide exchange factors (GEFs), specific for Rac or Cdc42. This approach allowed us to bypass extracellular signaling events and precisely manipulate localized GTPase activity.

The authors benchmarked iLID along with other light-inducible dimers in the field.

Furthermore, we benchmarked our dimer along with other light inducible dimers in the field.

The authors benchmarked iLID along with other light-inducible dimers in the field.

Furthermore, we benchmarked our dimer along with other light inducible dimers in the field.

The authors benchmarked iLID along with other light-inducible dimers in the field.

Furthermore, we benchmarked our dimer along with other light inducible dimers in the field.

The authors benchmarked iLID along with other light-inducible dimers in the field.

Furthermore, we benchmarked our dimer along with other light inducible dimers in the field.

The authors benchmarked iLID along with other light-inducible dimers in the field.

Furthermore, we benchmarked our dimer along with other light inducible dimers in the field.

The authors benchmarked iLID along with other light-inducible dimers in the field.

Furthermore, we benchmarked our dimer along with other light inducible dimers in the field.

The authors benchmarked iLID along with other light-inducible dimers in the field.

Furthermore, we benchmarked our dimer along with other light inducible dimers in the field.

Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.

Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.

Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.

Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.

Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.

Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.

Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.

Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.

Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.

Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.

Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.

Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.

Light-inducible dimers can be used to control protein localization and activity with high spatial and temporal resolution for cellular optogenetics.

Light-inducible dimers are powerful tools for cellular optogenetics, as they can be used to control the localization and activity of proteins with high spatial and temporal resolution.

Multiple iLID variants were designed and characterized with a broad range of binding affinities and kinetics.

Therefore, we designed and characterized multiple variants with a broad range of binding affinities and kinetics.

Multiple iLID variants were designed and characterized with a broad range of binding affinities and kinetics.

Therefore, we designed and characterized multiple variants with a broad range of binding affinities and kinetics.

Multiple iLID variants were designed and characterized with a broad range of binding affinities and kinetics.

Therefore, we designed and characterized multiple variants with a broad range of binding affinities and kinetics.

Multiple iLID variants were designed and characterized with a broad range of binding affinities and kinetics.

Therefore, we designed and characterized multiple variants with a broad range of binding affinities and kinetics.

Multiple iLID variants were designed and characterized with a broad range of binding affinities and kinetics.

Therefore, we designed and characterized multiple variants with a broad range of binding affinities and kinetics.

Multiple iLID variants were designed and characterized with a broad range of binding affinities and kinetics.

Therefore, we designed and characterized multiple variants with a broad range of binding affinities and kinetics.

Multiple iLID variants were designed and characterized with a broad range of binding affinities and kinetics.

Therefore, we designed and characterized multiple variants with a broad range of binding affinities and kinetics.

CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.

We find that the switches vary dramatically in their dark and lit state binding affinities

CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.

We find that the switches vary dramatically in their dark and lit state binding affinities

CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.

We find that the switches vary dramatically in their dark and lit state binding affinities

CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.

We find that the switches vary dramatically in their dark and lit state binding affinities

CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.

We find that the switches vary dramatically in their dark and lit state binding affinities

CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.

We find that the switches vary dramatically in their dark and lit state binding affinities

CRY2/CIB1, iLID/SspB, and LOVpep/ePDZb vary dramatically in their dark-state and lit-state binding affinities.

We find that the switches vary dramatically in their dark and lit state binding affinities

opto-iTrkA is compatible with multi-day and population-level activation of TrkA in PC12 cells.

We further show with our opto-iTrkA that the system is compatible with multi-day and population-level activation of TrkA in PC12 cells.

opto-iTrkA is compatible with multi-day and population-level activation of TrkA in PC12 cells.

We further show with our opto-iTrkA that the system is compatible with multi-day and population-level activation of TrkA in PC12 cells.

opto-iTrkA is compatible with multi-day and population-level activation of TrkA in PC12 cells.

We further show with our opto-iTrkA that the system is compatible with multi-day and population-level activation of TrkA in PC12 cells.

opto-iTrkA is compatible with multi-day and population-level activation of TrkA in PC12 cells.

We further show with our opto-iTrkA that the system is compatible with multi-day and population-level activation of TrkA in PC12 cells.

opto-iTrkA is compatible with multi-day and population-level activation of TrkA in PC12 cells.

We further show with our opto-iTrkA that the system is compatible with multi-day and population-level activation of TrkA in PC12 cells.

opto-iTrkA is compatible with multi-day and population-level activation of TrkA in PC12 cells.

We further show with our opto-iTrkA that the system is compatible with multi-day and population-level activation of TrkA in PC12 cells.

opto-iTrkA is compatible with multi-day and population-level activation of TrkA in PC12 cells.

We further show with our opto-iTrkA that the system is compatible with multi-day and population-level activation of TrkA in PC12 cells.

Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.

we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...

Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.

we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...

Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.

we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...

Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.

we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...

Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.

we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...

Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.

we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...

Binding affinities of the examined blue-light-inducible dimers correlate with in vivo function measured by colocalization and functional assays.

we examined the biophysical and biochemical properties of three blue-light-inducible dimer variants ... and correlated these characteristics to in vivo colocalization and functional assays. We find that the switches vary dramatically in their dark and lit state binding affinities and that these affinities co...

Cells expressing the Rac-specific optogenetic GEF and plated on Poly-L-Lysine migrated randomly in a light gradient.

We found that cells expressing the optogenetic GEF specific for Rac, plated on Poly-L-Lysine (abolishing integrin based adhesion) migrate randomly in a gradient of light.

Cells expressing the Rac-specific optogenetic GEF and plated on Poly-L-Lysine migrated randomly in a light gradient.

We found that cells expressing the optogenetic GEF specific for Rac, plated on Poly-L-Lysine (abolishing integrin based adhesion) migrate randomly in a gradient of light.

Cells expressing the Rac-specific optogenetic GEF and plated on Poly-L-Lysine migrated randomly in a light gradient.

We found that cells expressing the optogenetic GEF specific for Rac, plated on Poly-L-Lysine (abolishing integrin based adhesion) migrate randomly in a gradient of light.

Cells expressing the Rac-specific optogenetic GEF and plated on Poly-L-Lysine migrated randomly in a light gradient.

We found that cells expressing the optogenetic GEF specific for Rac, plated on Poly-L-Lysine (abolishing integrin based adhesion) migrate randomly in a gradient of light.

Cells expressing the Rac-specific optogenetic GEF and plated on Poly-L-Lysine migrated randomly in a light gradient.

We found that cells expressing the optogenetic GEF specific for Rac, plated on Poly-L-Lysine (abolishing integrin based adhesion) migrate randomly in a gradient of light.

Cells expressing the Rac-specific optogenetic GEF and plated on Poly-L-Lysine migrated randomly in a light gradient.

We found that cells expressing the optogenetic GEF specific for Rac, plated on Poly-L-Lysine (abolishing integrin based adhesion) migrate randomly in a gradient of light.

Cells expressing the Rac-specific optogenetic GEF and plated on Poly-L-Lysine migrated randomly in a light gradient.

We found that cells expressing the optogenetic GEF specific for Rac, plated on Poly-L-Lysine (abolishing integrin based adhesion) migrate randomly in a gradient of light.

iLID is an engineered light-inducible dimer that provides spatial and temporal control of signaling by modulating protein-protein interactions.

We have therefore engineered a light inducible dimer (iLID) that provides spatial and temporal control of signaling by modulating protein-protein interactions.

iLID is an engineered light-inducible dimer that provides spatial and temporal control of signaling by modulating protein-protein interactions.

We have therefore engineered a light inducible dimer (iLID) that provides spatial and temporal control of signaling by modulating protein-protein interactions.

iLID is an engineered light-inducible dimer that provides spatial and temporal control of signaling by modulating protein-protein interactions.

We have therefore engineered a light inducible dimer (iLID) that provides spatial and temporal control of signaling by modulating protein-protein interactions.

iLID is an engineered light-inducible dimer that provides spatial and temporal control of signaling by modulating protein-protein interactions.

We have therefore engineered a light inducible dimer (iLID) that provides spatial and temporal control of signaling by modulating protein-protein interactions.

iLID is an engineered light-inducible dimer that provides spatial and temporal control of signaling by modulating protein-protein interactions.

We have therefore engineered a light inducible dimer (iLID) that provides spatial and temporal control of signaling by modulating protein-protein interactions.

iLID is an engineered light-inducible dimer that provides spatial and temporal control of signaling by modulating protein-protein interactions.

We have therefore engineered a light inducible dimer (iLID) that provides spatial and temporal control of signaling by modulating protein-protein interactions.

iLID is an engineered light-inducible dimer that provides spatial and temporal control of signaling by modulating protein-protein interactions.

We have therefore engineered a light inducible dimer (iLID) that provides spatial and temporal control of signaling by modulating protein-protein interactions.

Cells expressing either optogenetic GEF and plated on fibronectin migrated up a light gradient.

We first hypothesized and verified that cells expressing either optogenetic GEF, plated on fibronectin and exposed to a gradient of light would migrate up the gradient or “phototax”.

Cells expressing either optogenetic GEF and plated on fibronectin migrated up a light gradient.

We first hypothesized and verified that cells expressing either optogenetic GEF, plated on fibronectin and exposed to a gradient of light would migrate up the gradient or “phototax”.

Cells expressing either optogenetic GEF and plated on fibronectin migrated up a light gradient.

We first hypothesized and verified that cells expressing either optogenetic GEF, plated on fibronectin and exposed to a gradient of light would migrate up the gradient or “phototax”.

Cells expressing either optogenetic GEF and plated on fibronectin migrated up a light gradient.

We first hypothesized and verified that cells expressing either optogenetic GEF, plated on fibronectin and exposed to a gradient of light would migrate up the gradient or “phototax”.

Cells expressing either optogenetic GEF and plated on fibronectin migrated up a light gradient.

We first hypothesized and verified that cells expressing either optogenetic GEF, plated on fibronectin and exposed to a gradient of light would migrate up the gradient or “phototax”.

Cells expressing either optogenetic GEF and plated on fibronectin migrated up a light gradient.

We first hypothesized and verified that cells expressing either optogenetic GEF, plated on fibronectin and exposed to a gradient of light would migrate up the gradient or “phototax”.

Cells expressing either optogenetic GEF and plated on fibronectin migrated up a light gradient.

We first hypothesized and verified that cells expressing either optogenetic GEF, plated on fibronectin and exposed to a gradient of light would migrate up the gradient or “phototax”.

Cells expressing the Cdc42-specific optogenetic GEF moved directionally in a light gradient independent of a fibronectin substrate.

Interestingly, we find that cells expressing the optogenetic GEF specific for Cdc42 move directionally in a gradient of light independent of a fibronectin substrate.

Cells expressing the Cdc42-specific optogenetic GEF moved directionally in a light gradient independent of a fibronectin substrate.

Interestingly, we find that cells expressing the optogenetic GEF specific for Cdc42 move directionally in a gradient of light independent of a fibronectin substrate.

Cells expressing the Cdc42-specific optogenetic GEF moved directionally in a light gradient independent of a fibronectin substrate.

Interestingly, we find that cells expressing the optogenetic GEF specific for Cdc42 move directionally in a gradient of light independent of a fibronectin substrate.

Cells expressing the Cdc42-specific optogenetic GEF moved directionally in a light gradient independent of a fibronectin substrate.

Interestingly, we find that cells expressing the optogenetic GEF specific for Cdc42 move directionally in a gradient of light independent of a fibronectin substrate.

Cells expressing the Cdc42-specific optogenetic GEF moved directionally in a light gradient independent of a fibronectin substrate.

Interestingly, we find that cells expressing the optogenetic GEF specific for Cdc42 move directionally in a gradient of light independent of a fibronectin substrate.

Cells expressing the Cdc42-specific optogenetic GEF moved directionally in a light gradient independent of a fibronectin substrate.

Interestingly, we find that cells expressing the optogenetic GEF specific for Cdc42 move directionally in a gradient of light independent of a fibronectin substrate.

Cells expressing the Cdc42-specific optogenetic GEF moved directionally in a light gradient independent of a fibronectin substrate.

Interestingly, we find that cells expressing the optogenetic GEF specific for Cdc42 move directionally in a gradient of light independent of a fibronectin substrate.

In the absence of light, iLID-RTK is cytosolic, monomeric, and inactive.

In the absence of light, the iLID-RTK is cytosolic, monomeric and inactive.

In the absence of light, iLID-RTK is cytosolic, monomeric, and inactive.

In the absence of light, the iLID-RTK is cytosolic, monomeric and inactive.

In the absence of light, iLID-RTK is cytosolic, monomeric, and inactive.

In the absence of light, the iLID-RTK is cytosolic, monomeric and inactive.

In the absence of light, iLID-RTK is cytosolic, monomeric, and inactive.

In the absence of light, the iLID-RTK is cytosolic, monomeric and inactive.

In the absence of light, iLID-RTK is cytosolic, monomeric, and inactive.

In the absence of light, the iLID-RTK is cytosolic, monomeric and inactive.

In the absence of light, iLID-RTK is cytosolic, monomeric, and inactive.

In the absence of light, the iLID-RTK is cytosolic, monomeric and inactive.

In the absence of light, iLID-RTK is cytosolic, monomeric, and inactive.

In the absence of light, the iLID-RTK is cytosolic, monomeric and inactive.

Under blue light, the iLID plus tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID + tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID plus tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID + tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID plus tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID + tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID plus tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID + tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID plus tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID + tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID plus tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID + tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID plus tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Under blue light, the iLID + tdnano system recruits two copies of iLID-RTK to tdnano, dimerizing and activating the RTK.

Cdc42-dependent secretion of fibronectin under newly formed protrusions stabilizes lamellipodia and provides feedback necessary for directional migration.

Through further optogenetic experiments, we show that this is due to a Cdc42 dependent secretion of fibronectin under newly formed protrusions, stabilizing the lamellipodia and providing the necessary feedback for directional migration.

Cdc42-dependent secretion of fibronectin under newly formed protrusions stabilizes lamellipodia and provides feedback necessary for directional migration.

Through further optogenetic experiments, we show that this is due to a Cdc42 dependent secretion of fibronectin under newly formed protrusions, stabilizing the lamellipodia and providing the necessary feedback for directional migration.

Cdc42-dependent secretion of fibronectin under newly formed protrusions stabilizes lamellipodia and provides feedback necessary for directional migration.

Through further optogenetic experiments, we show that this is due to a Cdc42 dependent secretion of fibronectin under newly formed protrusions, stabilizing the lamellipodia and providing the necessary feedback for directional migration.

Cdc42-dependent secretion of fibronectin under newly formed protrusions stabilizes lamellipodia and provides feedback necessary for directional migration.

Through further optogenetic experiments, we show that this is due to a Cdc42 dependent secretion of fibronectin under newly formed protrusions, stabilizing the lamellipodia and providing the necessary feedback for directional migration.

Cdc42-dependent secretion of fibronectin under newly formed protrusions stabilizes lamellipodia and provides feedback necessary for directional migration.

Through further optogenetic experiments, we show that this is due to a Cdc42 dependent secretion of fibronectin under newly formed protrusions, stabilizing the lamellipodia and providing the necessary feedback for directional migration.

Cdc42-dependent secretion of fibronectin under newly formed protrusions stabilizes lamellipodia and provides feedback necessary for directional migration.

Through further optogenetic experiments, we show that this is due to a Cdc42 dependent secretion of fibronectin under newly formed protrusions, stabilizing the lamellipodia and providing the necessary feedback for directional migration.

Cdc42-dependent secretion of fibronectin under newly formed protrusions stabilizes lamellipodia and provides feedback necessary for directional migration.

Through further optogenetic experiments, we show that this is due to a Cdc42 dependent secretion of fibronectin under newly formed protrusions, stabilizing the lamellipodia and providing the necessary feedback for directional migration.

Integrin-based adhesions provide signaling feedback within optogenetically formed protrusions that reinforces signals necessary for directed migration.

We provide evidence that integrin based adhesions provide signaling feedback within the optogenetically formed protrusions that reinforce the signals necessary for directed migration.

Integrin-based adhesions provide signaling feedback within optogenetically formed protrusions that reinforces signals necessary for directed migration.

We provide evidence that integrin based adhesions provide signaling feedback within the optogenetically formed protrusions that reinforce the signals necessary for directed migration.

Integrin-based adhesions provide signaling feedback within optogenetically formed protrusions that reinforces signals necessary for directed migration.

We provide evidence that integrin based adhesions provide signaling feedback within the optogenetically formed protrusions that reinforce the signals necessary for directed migration.

Integrin-based adhesions provide signaling feedback within optogenetically formed protrusions that reinforces signals necessary for directed migration.

We provide evidence that integrin based adhesions provide signaling feedback within the optogenetically formed protrusions that reinforce the signals necessary for directed migration.

Integrin-based adhesions provide signaling feedback within optogenetically formed protrusions that reinforces signals necessary for directed migration.

We provide evidence that integrin based adhesions provide signaling feedback within the optogenetically formed protrusions that reinforce the signals necessary for directed migration.

Integrin-based adhesions provide signaling feedback within optogenetically formed protrusions that reinforces signals necessary for directed migration.

We provide evidence that integrin based adhesions provide signaling feedback within the optogenetically formed protrusions that reinforce the signals necessary for directed migration.

Integrin-based adhesions provide signaling feedback within optogenetically formed protrusions that reinforces signals necessary for directed migration.

We provide evidence that integrin based adhesions provide signaling feedback within the optogenetically formed protrusions that reinforce the signals necessary for directed migration.

Genetic targeting of tdnano enables RTK activation at a specific subcellular location even with whole-cell illumination.

By leveraging genetic targeting of tdnano, we achieve RTK activation at a specific subcellular location even with whole-cell illumination

Genetic targeting of tdnano enables RTK activation at a specific subcellular location even with whole-cell illumination.

By leveraging genetic targeting of tdnano, we achieve RTK activation at a specific subcellular location even with whole-cell illumination

Genetic targeting of tdnano enables RTK activation at a specific subcellular location even with whole-cell illumination.

By leveraging genetic targeting of tdnano, we achieve RTK activation at a specific subcellular location even with whole-cell illumination

Genetic targeting of tdnano enables RTK activation at a specific subcellular location even with whole-cell illumination.

By leveraging genetic targeting of tdnano, we achieve RTK activation at a specific subcellular location even with whole-cell illumination

Genetic targeting of tdnano enables RTK activation at a specific subcellular location even with whole-cell illumination.

By leveraging genetic targeting of tdnano, we achieve RTK activation at a specific subcellular location even with whole-cell illumination

Genetic targeting of tdnano enables RTK activation at a specific subcellular location even with whole-cell illumination.

By leveraging genetic targeting of tdnano, we achieve RTK activation at a specific subcellular location even with whole-cell illumination

Genetic targeting of tdnano enables RTK activation at a specific subcellular location even with whole-cell illumination.

By leveraging genetic targeting of tdnano, we achieve RTK activation at a specific subcellular location even with whole-cell illumination

iLID is a LOV2-based light-induced dimerization system that controls localization and activity through light-driven conformational exposure of an embedded peptide.

LOVTRAP is a reversible photoinduced dissociation system that uses state-selective binding to LOV2 for sequestration and release.

pdDronpa can be used as a photodissociable component to cage and uncage protein activity in direct conformational control designs.

Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.

Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.

Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.

Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.

Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.

Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.

Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.

Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.

Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.

Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.

Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.

Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.

Cry2/CIB1, iLID, and Magnets were compared for the extent of light-dependent dimer occurrence in small subcellular volumes.

Here, we compared and quantified the extent of light-dependent dimer occurrence in small, subcellular volumes controlled by three such tools: Cry2/CIB1, iLID, and Magnets.

Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of light-induced dimerization to the illuminated area is achieved when the photosensitive component is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

Efficient spatial confinement of dimer to the area of illumination is achieved when the photosensitive component of the dimerization pair is tethered to the membrane of intracellular compartments and when on and off kinetics are extremely fast, as achieved with iLID or Magnets.

The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.

We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.

The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.

We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.

The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.

We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.

The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.

We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.

The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.

We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.

The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.

We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.

The location of the photoreceptor protein in the dimer pair and its switch-off kinetics determine the subcellular volume of dimer formation and the amount of protein recruited in the illuminated volume.

We show that both the location of the photoreceptor protein(s) in the dimer pair and its (their) switch-off kinetics determine the subcellular volume where dimer formation occurs and the amount of protein recruited in the illuminated volume.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, but with reduced total amount of dimer.

Magnets and the iLID variants with the fastest switch-off kinetics induce and maintain protein dimerization in the smallest volume, although this comes at the expense of the total amount of dimer.

SxIP-iLID can temporally recruit an F-actin binding domain to microtubule plus ends and cross-link the microtubule and F-actin networks.

We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks.

SxIP-iLID can temporally recruit an F-actin binding domain to microtubule plus ends and cross-link the microtubule and F-actin networks.

We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks.

SxIP-iLID can temporally recruit an F-actin binding domain to microtubule plus ends and cross-link the microtubule and F-actin networks.

We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks.

SxIP-iLID can temporally recruit an F-actin binding domain to microtubule plus ends and cross-link the microtubule and F-actin networks.

We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks.

SxIP-iLID can temporally recruit an F-actin binding domain to microtubule plus ends and cross-link the microtubule and F-actin networks.

We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks.

SxIP-iLID can temporally recruit an F-actin binding domain to microtubule plus ends and cross-link the microtubule and F-actin networks.

We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks.

SxIP-iLID can temporally recruit an F-actin binding domain to microtubule plus ends and cross-link the microtubule and F-actin networks.

We show that SxIP-iLID can be used to temporally recruit an F-actin binding domain to MT plus ends and cross-link the MT and F-actin networks.

SxIP-iLID facilitates general recruitment of specific factors to microtubule plus ends with temporal control for regulating microtubule plus end dynamics and probing microtubule plus end function.

SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

SxIP-iLID facilitates general recruitment of specific factors to microtubule plus ends with temporal control for regulating microtubule plus end dynamics and probing microtubule plus end function.

SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

SxIP-iLID facilitates general recruitment of specific factors to microtubule plus ends with temporal control for regulating microtubule plus end dynamics and probing microtubule plus end function.

SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

SxIP-iLID facilitates general recruitment of specific factors to microtubule plus ends with temporal control for regulating microtubule plus end dynamics and probing microtubule plus end function.

SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

SxIP-iLID facilitates general recruitment of specific factors to microtubule plus ends with temporal control for regulating microtubule plus end dynamics and probing microtubule plus end function.

SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

SxIP-iLID facilitates general recruitment of specific factors to microtubule plus ends with temporal control for regulating microtubule plus end dynamics and probing microtubule plus end function.

SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

SxIP-iLID facilitates general recruitment of specific factors to microtubule plus ends with temporal control for regulating microtubule plus end dynamics and probing microtubule plus end function.

SxIP-iLID facilitates the general recruitment of specific factors to MT plus ends with temporal control enabling researchers to systematically regulate MT plus end dynamics and probe MT plus end function in many biological processes.

SxIP-iLID can track microtubule plus ends and recruit tgRFP-SspB upon blue light activation.

We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation.

SxIP-iLID can track microtubule plus ends and recruit tgRFP-SspB upon blue light activation.

We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation.

SxIP-iLID can track microtubule plus ends and recruit tgRFP-SspB upon blue light activation.

We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation.

SxIP-iLID can track microtubule plus ends and recruit tgRFP-SspB upon blue light activation.

We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation.

SxIP-iLID can track microtubule plus ends and recruit tgRFP-SspB upon blue light activation.

We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation.

SxIP-iLID can track microtubule plus ends and recruit tgRFP-SspB upon blue light activation.

We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation.

SxIP-iLID can track microtubule plus ends and recruit tgRFP-SspB upon blue light activation.

We show that SxIP-iLID can track MT plus ends and recruit tgRFP-SspB upon blue light activation.

Cross-linking microtubule plus ends and F-actin decreases microtubule growth velocities and generates a peripheral microtubule exclusion zone.

Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone.

Cross-linking microtubule plus ends and F-actin decreases microtubule growth velocities and generates a peripheral microtubule exclusion zone.

Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone.

Cross-linking microtubule plus ends and F-actin decreases microtubule growth velocities and generates a peripheral microtubule exclusion zone.

Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone.

Cross-linking microtubule plus ends and F-actin decreases microtubule growth velocities and generates a peripheral microtubule exclusion zone.

Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone.

Cross-linking microtubule plus ends and F-actin decreases microtubule growth velocities and generates a peripheral microtubule exclusion zone.

Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone.

Cross-linking microtubule plus ends and F-actin decreases microtubule growth velocities and generates a peripheral microtubule exclusion zone.

Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone.

Cross-linking microtubule plus ends and F-actin decreases microtubule growth velocities and generates a peripheral microtubule exclusion zone.

Cross-linking decreases MT growth velocities and generates a peripheral MT exclusion zone.

SxIP-iLID facilitates reversible recruitment of factors to microtubule plus ends in an end-binding protein-dependent manner using blue light.

We developed a novel optogenetic tool, SxIP-improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein-dependent manner using blue light.

SxIP-iLID facilitates reversible recruitment of factors to microtubule plus ends in an end-binding protein-dependent manner using blue light.

We developed a novel optogenetic tool, SxIP-improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein-dependent manner using blue light.

SxIP-iLID facilitates reversible recruitment of factors to microtubule plus ends in an end-binding protein-dependent manner using blue light.

We developed a novel optogenetic tool, SxIP-improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein-dependent manner using blue light.

SxIP-iLID facilitates reversible recruitment of factors to microtubule plus ends in an end-binding protein-dependent manner using blue light.

We developed a novel optogenetic tool, SxIP-improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein-dependent manner using blue light.

SxIP-iLID facilitates reversible recruitment of factors to microtubule plus ends in an end-binding protein-dependent manner using blue light.

We developed a novel optogenetic tool, SxIP-improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein-dependent manner using blue light.

SxIP-iLID facilitates reversible recruitment of factors to microtubule plus ends in an end-binding protein-dependent manner using blue light.

We developed a novel optogenetic tool, SxIP-improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein-dependent manner using blue light.

SxIP-iLID facilitates reversible recruitment of factors to microtubule plus ends in an end-binding protein-dependent manner using blue light.

We developed a novel optogenetic tool, SxIP-improved light-inducible dimer (iLID), to facilitate the reversible recruitment of factors to microtubule (MT) plus ends in an end-binding protein-dependent manner using blue light.

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V-containing iLID dimer variant allows light-activated colocalization of transmembrane proteins in neurons, whereas a higher-affinity switch was less effective because it showed more colocalization in the dark.

allows for light-activated colocalization of transmembrane proteins in neurons, where a higher affinity switch (0.8-47 bcM) was less effective because more colocalization was seen in the dark

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The SspB A58V-containing iLID dimer variant displays a 42-fold light-dependent change in binding affinity, from 125 bcM in one state to 3 bcM in the activated blue-light state.

The new variant of the dimer system contains a single SspB point mutation (A58V), and displays a 42-fold change in binding affinity when activated with blue light (from 3 b1 2 bcM to 125 b1 40 bcM)

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

The iLID-SspB system was reengineered to better control proteins present at high effective concentrations of 5-100 bcM.

Here, we reengineer the interaction between the light inducible dimer, iLID, and its binding partner SspB, to better control proteins present at high effective concentrations (5-100 bcM).

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

A point mutation in the LOV domain, N414L, lengthened the reversion half-life of iLID.

Additionally, with a point mutation in the LOV domain (N414L), we lengthened the reversion half-life of iLID.

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.

iLID contains a LOV domain that undergoes a conformational change upon blue-light activation and exposes the ssrA peptide motif that binds SspB.

iLID contains a light-oxygen-voltage (LOV) domain that undergoes a conformational change upon activation with blue light and exposes a peptide motif, ssrA, that binds to SspB.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

The expanded suite of light-induced dimers increases the variety of cellular pathways that can be targeted with light.

This expanded suite of light induced dimers increases the variety of cellular pathways that can be targeted with light.

The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.

in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling

The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.

in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling

The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.

in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling

The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.

in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling

The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.

in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling

The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.

in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling

The examined dimers were evaluated in in vivo assays including transcription control, intracellular localization studies, and control of GTPase signaling.

in a variety of in vivo assays, including transcription control, intracellular localization studies, and control of GTPase signaling