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Biochem Biophys Res Commun. 2002 Feb 15;291(1):41-7.

WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation.

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Department of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan.


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.

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