Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as lamellipodial and filopodial dynamics in migrating cells. Plays a crucial role in filopodia formation, cell-substratum adhesion, and proper chemotaxis. Nucleates and bundles actin filaments. When complexed with fotH in filopodial tips, may support formin-mediated filament elongation by bundling nascent actin filaments. May self-associate (By similarity). Binds F-actin and G-actin (By similarity). Binds to the FH2 domain of forH. Localizes to the leading edge of migrating cells and to the tips of filipodia. Translocates to the cell cortex in response to cAMP chemoattractant stimulation. Expressed in vegatatively growing cells. Expression increases upon starvation from and remains high until fruiting body formation. The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding and actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for self-association (By similarity). Belongs to the Ena/VASP family.