EnaVASP

EnaVASP is a term used in molecular and cell biology to refer to the Ena/VASP protein family, a small group of actin-regulatory proteins that coordinate cytoskeletal dynamics and cell motility. In vertebrates this family comprises ENAH (also called Mena for multiple isoforms), VASP, and EVL. The proteins share a conserved modular architecture that includes an N-terminal EVH1 domain, a central proline-rich region, and a C-terminal EVH2 domain. The EVH1 domain binds polyproline-containing partner proteins, the EVH2 domain binds and promotes actin filament elongation, and the proline-rich region mediates interactions with profilin and other SH3-domain proteins. Together these features support targeted actin polymerization at sites of adhesion and protrusion, such as focal adhesions and filopodial tips, and also regulate filament capping and bundling.

Function and regulation: Ena/VASP proteins promote filament elongation by delivering profilin-bound actin monomers and by antagonizing capping proteins. Activity and localization are controlled by signaling pathways that include Rho family GTPases, Src-family kinases, and other kinases, as well as alternative splicing that yields tissue- or development-specific isoforms.

Biological and clinical relevance: They influence cell migration, neurite outgrowth, angiogenesis, and immune cell motility. Misregulation has been linked to developmental processes and, in some cancers, to metastatic potential. In literature, EnaVASP is sometimes used as a shorthand for the Ena/VASP family rather than a single protein.

See also: Ena/VASP family; ENAH/Mena; VASP; EVL; actin polymerization.