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

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.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Moreau V,Frischknecht F,Reckmann I,Vincentelli R,Rabut G,Stewart D,Way M

doi

10.1038/35017080

keywords:

subject

Has Abstract

pub_date

2000-07-01 00:00:00

pages

441-8

issue

7

eissn

1465-7392

issn

1476-4679

journal_volume

2

pub_type

杂志文章

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