Article abstract
Nature Cell Biology 2, 441 - 448 (2000)
Published online: 16 June 2000 | doi:10.1038/35017080
A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization
Violaine Moreau1,2,4, Friedrich Frischknecht1,4, Inge Reckmann1, Renaud Vincentelli1, Gwénaël Rabut1, Donn Stewart3 & Michael Way1
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.
- European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
- Current address: Laboratoire des Facteurs de Croissance et de la Differenciation Cellulaire, Universite Bordeaux I, Avenue des facultes, 33405 Talence, France
- National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, Maryland 20892, USA
- These authors contributed equally to this work
Correspondence to: Michael Way1 e-mail: Way@EMBL-Heidelberg.de
