Vinculin, an adapter protein in control of cell adhesion signalling

Abstract

Vinculin, discovered in 1979 (Geiger, 1979), is an adapter protein with binding sites for more than 15 proteins. Biochemical and structural analyses have contributed to detailed knowledge about potential binding partners and the understanding of how their binding may be regulated. Despite all this information the molecular basis of how vinculin acts in cells and controls a wide variety of signals remains elusive. This review aims to highlight recent discoveries with an emphasis on how vinculin is involved in the coordination of a network of signals.

Role of the actin-binding protein profilin1 in radial migration and glial cell adhesion of granule neurons in the cerebellum

“…Vinculin is expressed in cell contacts of a variety of cell types, including neurons, [52][53][54] where it strengthens the mechanical link between cell-cell adhesion receptors and the actin cytoskeleton. 55 The functional link of profilin1 to cell-cell contact formation is further confirmed by the reduced Mena localization to CGN-glial cell junctions in response to profilin1 inactivation. Mena is a member of the Ena/VASP protein family that is critical for the formation of cell-cell contacts in various cell types.…”

Association of Nox1 and Vinculin With Colon Cancer Progression

“…Vinculin is a molecule localized at cell-cell junction and plays a key role in controlling cell motility (26). vinculin exhibits very different function in 2D and 3D cell culture models: in 2D model, less vinculin renders cells to become more motile and more invasive; however, in 3D model, the outcome is opposite: more vinculin renders cells more invasive (27).…”

The β1-integrin-p-FAK-p130Cas-DOCK180-RhoA-vinculin is a novel regulatory protein complex at the apical ectoplasmic specialization in adult rat testes

“…48,49 However, we have shown herein that vinculin is also a component of the basal ES at the BTB besides it intense stage-specific expression and localization at the apical ES. Collectively, p130Cas, DOCK180, RhoA and vinculin [and their associated partners, such as Crk, R-ras (a GTPase involved in Rho signaling, regulating actin dynamics 50,51 ) and Grb2 (growth factor receptor-bound protein 2, also an adaptor involved in the p130Cas/DOCK180 signaling 52,53 )] are putative components of the β1-integrin-based adhesion protein complex at the apical ES in the seminiferous epithelium.…”