Source 1primary paper2025Chemical Science
Toolkit/nano
nano
Also known as: wild-type SspB
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
nano is the wild-type SspB protein used as the binding partner for iLID in a blue-light-responsive dimerization system. In the cited work, the iLID–nano pair is used to control protein interactions and localization with light.
Usefulness & Problems
Why this is useful
nano is useful as the cognate binding partner in the iLID optogenetic system, enabling light-dependent recruitment and localization control. The cited literature specifically supports its use in photoswitchable interaction schemes at model membranes and in light-guided synthetic cell behaviors.
Source:
Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.
Source:
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)
Source:
Here, a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision.
Source:
a method is described for fabricating light-regulated reversible protein patterns at lipid membranes with high spatiotemporal precision
Problem solved
nano helps solve the problem of achieving externally controlled, spatially and temporally precise protein localization through a photoswitchable binding interaction with iLID. The associated design-rule literature further indicates that such light-controlled ligand-receptor interactions can be tuned to support reversible adhesion asymmetry and guided motility in synthetic membrane systems.
Source:
Overall, this is a flexible and versatile method for regulating the localization of proteins with high precision in space and time using blue light.
Source:
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)
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
HeterodimerizationTechniques
Computational DesignTarget processes
localizationInput: Light
Implementation Constraints
Implementation requires pairing nano with iLID as the interacting optogenetic partner in a light-controlled construct. The provided evidence does not specify construct architecture, cofactors, expression host, delivery method, or illumination wavelength beyond the general designation of a photoswitchable light-inducible dimerization system.
The supplied evidence only establishes nano as wild-type SspB that binds iLID in a photoswitchable system, without standalone biochemical characterization. The design-rule claims concern ligand density and mobility in synthetic membrane motility assays rather than direct engineering or comparative performance of nano itself.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2024Journal of Visualized Experiments
Source 3primary paper2024
Ranked Claims
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.
Approval Evidence
3 sources10 linked approval claimsfirst-pass slug nano
we use the photoswitchable interactions between the proteins iLID (improved light-inducible dimer) and nano (wild-type SspB)
Source:
iLID binds to its partner Nano (wild-type SspB)
Source:
iLID binds to its partner Nano (wild-type SspB)
Source:
design rulesupports
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.
Source:
design rulesupports
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.
Source:
mechanistic effectsupports
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.
Source:
application scopesupports
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.
Source:
binding mechanismsupports
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.
Source:
binding responsesupports
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.
Source:
method capabilitysupports
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.
Source:
method capabilitysupports
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
Source:
reversibilitysupports
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.
Source:
reversibilitysupports
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.
Source:
Comparisons
Source-backed strengths
The evidence supports that nano functions as the wild-type SspB partner of iLID in a photoswitchable interaction system. The cited context indicates utility for localized illumination experiments and dynamic protein patterning, but the provided evidence does not include quantitative binding, kinetics, or performance benchmarks for nano alone.
Ranked Citations
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