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1: Nat Cell Biol. 2000 Jul;2(7):441-8.Click here to read Links

A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization.

Moreau V, Frischknecht F, Reckmann I, Vincentelli R, Rabut G, Stewart D, Way M.

European Molecular Biology Laboratory, Heidelberg, Germany.

Wiskott-Aldrich syndrome protein (WASP) and N-WASP have emerged as key proteins connecting signalling cascades to actin polymerization. Here we show that the amino-terminal WH1 domain, and not the polyproline-rich region, of N-WASP is responsible for its recruitment to sites of actin polymerization during Cdc42-independent, actin-based motility of vaccinia virus. Recruitment of N-WASP to vaccinia is mediated by WASP-interacting protein (WIP), whereas in Shigella WIP is recruited by N-WASP. Our observations show that vaccinia and Shigella activate the Arp2/3 complex to achieve actin-based motility, by mimicking either the SH2/SH3-containing adaptor or Cdc42 signalling pathways to recruit the N-WASP-WIP complex. We propose that the N-WASP-WIP complex has a pivotal function in integrating signalling cascades that lead to actin polymerization.

PMID: 10878810 [PubMed - indexed for MEDLINE]