WICH, a Novel Verprolin Homology Domain-Containing Protein That Functions Cooperatively with N-WASP in Actin-Microspike Formation

We describe a novel protein that contains a verprolin-homology (V) region, through which several actin-regulating proteins, including Wiskott–Aldrich syndrome protein (WASP) family members, bind directly to actin. The amino acid sequence is homologous to the sequences of WASP-interacting protein (WIP) and CR16, both of which associate with WASP and/or N-WASP, and thus these three proteins constitute a new protein family. We named the protein WICH (WIP- and CR16-homologous protein). WICH associates strongly with N-WASP but only weakly with WASP via its C-terminal WASP-interacting (W) region. Ectopic expression of WICH induces actin-microspike formation through cooperation with N-WASP. In addition, expression of the W fragment of WICH suppresses microspike formation induced by N-WASP, indicating an essential role for WICH in N-WASP-induced microspike formation.