Ena/VASP-like protein is a member of the Ena/VASP family and is involved in actin-associated cytoskeleton remodeling and cell polarity activities including axon guidance and lamellipodia formation in migrating cells. The EVL protein sequence contains an N-terminal EVH1 domain, a Pro-rich SH3 binding domain, and a C-terminal EVH2 domain. EVL domain interactions with G- and F-actin mediates actin nucleation and polymerization. Research studies have shown that EVL also regulates DNA repair by direct interaction with RAD51. EVL may function in the DSB repair pathway through the EVH2 domain, which possesses DNA-binding and RAD51 binding activity, thereby coordinating homologous DNA recombination. Research studies have shown EVL expression is up-regulated in human breast cancer associated with clinical stages and may be implicated in invasion and/or metastasis of human breast cancer.
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