WAVE and Arp2/3 jointly inhibit filopodium formation by entering into a complex with mDia2.
Nat Cell Biol
; 10(7): 849-57, 2008 Jul.
Article
en En
| MEDLINE
| ID: mdl-18516090
ABSTRACT
Lamellipodia/ruffles and filopodia are protruding organelles containing short and highly branched or long and unbranched actin filaments, respectively. The microscopic morphology, dynamic development and protein signature of both lamellipodia/ruffles and filopodia have been investigated; however, little is known about the mechanisms by which cells coordinate the formation of these actin-based extensions. Here, we show that WAVE holds mDia2 and the Arp2/3 complex in a multimolecular complex. WAVE- and Arp2/3-dependent ruffling induced by EGF does not require mDia2. Conversely, the emission of mDia2-dependent filopodia correlates with its disengagement from WAVE. Consistently, the ability of EGF, Cdc42 and serum to induce mDia2-dependent formation of filopodia is increased in the absence of either the WAVE/Abi1/Nap1/PIR121 (WANP) or the Arp2/3 complex. Reintroduction of WAVE2 into WANP-complex knockdown cells markedly reduces filopodia formation independently of actin polymerization. Thus, WAVE and the Arp2/3 complex jointly orchestrate different types of actin-based plasma membrane protrusions by promoting ruffling and inhibiting mDia2-induced filopodia.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Seudópodos
/
Proteínas Portadoras
/
Complejos Multiproteicos
/
Complejo 2-3 Proteico Relacionado con la Actina
/
Familia de Proteínas del Síndrome de Wiskott-Aldrich
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Nat Cell Biol
Año:
2008
Tipo del documento:
Article
País de afiliación:
Alemania