A Structural Model for Vinculin Insertion into PIP₂-Containing Membranes and the Effect of Insertion on Vinculin Activation and Localization.

ABSTRACT: Vinculin, a scaffolding protein that localizes to focal adhesions (FAs) and adherens junctions, links the actin cytoskeleton to the adhesive super-structure. While vinculin binds to a number of cytoskeletal proteins, it can also associate with phosphatidylinositol 4,5-bisphosphate (PIP₂) to drive membrane association. To generate a structural model for PIP₂-dependent interaction of vinculin with the lipid bilayer, we conducted lipid-association, nuclear magnetic resonance, and computational modeling experiments. We find that two basic patches on the vinculin tail drive membrane association: the basic collar specifically recognizes PIP₂, while the basic ladder drives association with the lipid bilayer. Vinculin mutants with defects in PIP₂-depende

SUBMITTER: Thompson PM 

PROVIDER: S-EPMC5299030 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature