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A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization.
Moreau, V; Frischknecht, F; Reckmann, I; Vincentelli, R; Rabut, G; Stewart, D; Way, M.
Afiliación
  • Moreau V; European Molecular Biology Laboratory, Heidelberg, Germany.
Nat Cell Biol ; 2(7): 441-8, 2000 Jul.
Article en En | MEDLINE | ID: mdl-10878810
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.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Citoesqueleto de Actina / Transducción de Señal / Proteínas Portadoras / Actinas / Proteínas del Tejido Nervioso Límite: Humans Idioma: En Revista: Nat Cell Biol Año: 2000 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Citoesqueleto de Actina / Transducción de Señal / Proteínas Portadoras / Actinas / Proteínas del Tejido Nervioso Límite: Humans Idioma: En Revista: Nat Cell Biol Año: 2000 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido