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. 2000 Jul;2(7):441-8.
doi: 10.1038/35017080.

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

V Moreau  1 , F Frischknecht, I Reckmann, R Vincentelli, G Rabut, D Stewart, M Way
Affiliations

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

V Moreau et al. Nat Cell Biol. 2000 Jul.

Abstract

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.

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