iLID

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

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

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

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 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 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.

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

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

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