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

被引：0
作者：
Violaine Moreau
Friedrich Frischknecht
Inge Reckmann
Renaud Vincentelli
Gwénaël Rabut
Donn Stewart
Michael Way
机构：
[1] European Molecular Biology Laboratory,Laboratoire des Facteurs de Croissance et de la Differenciation Cellulaire
[2] National Cancer Institute,undefined
[3] National Institutes of Health,undefined
[4] Universite Bordeaux I,undefined
来源：
Nature Cell Biology | 2000年 / 2卷
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摘要：
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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页码：441 / 448
页数：7
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