A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization
Author: ["Violaine Moreau","Friedrich Frischknecht","Inge Reckmann","Renaud Vincentelli","Gwénaël Rabut","Donn Stewart","Michael Way"]
Publication: Nature Cell Biology
CITE.CC academic search helps you expand the influence of your papers.
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.
Cite this article
Moreau, V., Frischknecht, F., Reckmann, I. et al. A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat Cell Biol 2, 441–448 (2000). https://doi.org/10.1038/35017080
