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 |
| |
Institution: | European Molecular Biology Laboratory, Heidelberg, Germany. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|