We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization.
- Authors
Moreau, V; Frischknecht, F; Reckmann, I; Vincentelli, R; Rabut, G; Stewart, D; Way, M
- 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.
- Publication
Nature cell biology, 2000, Vol 2, Issue 7, p441
- ISSN
1465-7392
- Publication type
Journal Article
- DOI
10.1038/35017080