evl

EVL is commonly used to refer to Ena/VASP-like protein, a member of the Ena/VASP family of actin-regulatory proteins. In humans, the EVL gene encodes this cytoskeletal protein, which localizes to dynamic actin structures such as lamellipodia and filopodia and participates in the regulation of actin filament elongation and remodeling.

The EVL protein features an N-terminal EVH1 domain, a central proline-rich region, and a C-terminal EVH2 domain. These domains enable interactions with actin and with profilin-family proteins, supporting processes that shape the cytoskeleton. Through these interactions, EVL contributes to cellular activities including migration, adhesion, and morphological changes in developing and responding tissues. EVL is expressed broadly, with notable presence in vascular and neural contexts, and it is thought to function in concert with other Ena/VASP family members under various signaling conditions.

Functionally, EVL influences actin polymerization dynamics and the organization of actin structures at the leading edge of migrating cells and at focal adhesions. Its activity is integrated with signaling pathways that regulate the cytoskeleton, such as those mediated by Rho family GTPases and cyclic nucleotide signaling, coordinating cellular movement and shape changes.

Clinical significance for EVL is less defined than for some related proteins. While Ena/VASP proteins have been linked to cell motility in cancer and to vascular development in experimental systems, there is no single disease universally attributed to EVL dysfunction. Research continues to clarify its roles in endothelial function, neural development, and tissue morphogenesis.

EVL can also refer to other uses as an acronym in different disciplines; in biological literature, however, it most commonly denotes the Ena/VASP-like protein encoded by the EVL gene.