WAS Protein Family Homolog 7 (WASH7)

WASH has 2 WASH homology domains (WHD1 and WHD2) in its N-terminal half. In its C-terminal half, WASH has a proline-rich stretch followed by a WH2 actin-binding domain (V), a central region (C), and an acidic stretch (A) that together form the VCA module found in all WASP proteins. Database analysis revealed WASH orthologs in both vertebrates and invertebrates. Vertebrates showed highest conservation in the WASH C terminus. Fluorescence-tagged WASH1 colocalized with cytoskeletal actin and accumulated in filopodia and lamellipodia. Component of the WASH complex, a complex present at the surface of endosomes that recruits and activates the Arp2/3 complex to induce actin polymerization. The WASH complex plays a key role in the fission of tubules that serve as transport intermediates during endosome sorting.