Vinculin (VCL)

Vinculin is a 117-kDa cytoskeletal actin-binding protein, highly conserved and ubiquitously expressed, comprising a head domain (binding talin, α-actinin, catenins), a proline-rich linker, and a tail domain (binding actin, paxillin, PIP2). Vinculin exists in closed (inactive) and open (active) conformations, mediating its ability to connect adhesion receptors on the membrane—primarily integrins—to the dynamic actin cytoskeleton. This connection stabilizes focal adhesions and adherens junctions, influences cell shape, regulates migration, and transmits mechanical signals. Metavinculin is a cardiac isoform with additional protein sequence and disease relevance. Disruption of vinculin impacts cell adhesion, migration, and can contribute to disease such as cancer and cardiomyopathy.

Other names

MetavinculinMVVINCCMD1WCMH15HEL114MVCLepididymis luminal protein 114epididymis secretory sperm binding proteinmeta-vinculin

Not applicable for drugs (no direct therapeutic targeting). Vinculin functions through conformational change (inactive/active states), regulated by ligand binding (e.g., talin, α-actinin, actin), and phosphorylation