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