Molecular basis for differential PIP₂-mediated association between vinculin and its splice isoform metavinculin.

ABSTRACT: Vinculin (Vcn) and its splice variant metavinculin (MVcn) are cell adhesion proteins that regulate cell morphology, adhesion, and motility. They function as scaffold proteins that anchor membrane receptors to filamentous actin (F-actin) at focal adhesions and cell-cell junctions. MVcn bears an extra 68 amino acid insert in the tail domain and is selectively expressed in cardiac and smooth muscle cells at substoichiometric levels relative to Vcn. Mutations in the MVcn tail domain (MVt) promote cardiomyopathy, yet how these mutations alter ligand interactions to promote defects in force transduction and reduced blood flow is unclear. One difference between Vcn and MVcn lies in the ability to reorganize F-actin, with MVcn negatively regulating Vcn-mediated F-actin bundling. Vcn associates wit

SUBMITTER: Khan MAI 

PROVIDER: S-EPMC12180986 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature