WIP regulates N-WASP-mediated actin polymerization and filopodium formation

被引：228

作者：

Martinez-Quiles, N

Rohatgi, R

Antón, IM

Medina, M

Saville, SP

Miki, H

Yamaguchi, H

Takenawa, T

Hartwig, JH

Geha, RS

Ramesh, N

机构：

[1] Childrens Hosp, Div Immunol, Boston, MA 02115 USA

[2] Brigham & Womens Hosp, Div Expt Med, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Pediat, Boston, MA 02115 USA

[4] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

[5] Harvard Univ, Sch Med, Dept Neurol, Boston, MA 02115 USA

[6] Harvard Univ, Sch Med, Dept Med, Boston, MA 02115 USA

[7] Univ Tokyo, Inst Med Sci, Dept Biochem, Tokyo 108, Japan

来源：

NATURE CELL BIOLOGY | 2001年 / 3卷 / 05期

关键词：

D O I：

10.1038/35074551

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Induction of filopodia is dependent on activation of the small GTPase Cdc42 and on neural Wiskott-Aldrich-syndrome protein (N-WASP). Here we show that WASP-interacting protein (WIP) interacts directly with N-WASP and actin. WIP retards N-WASP/Cdc42-activated actin polymerization mediated by the Arp2/3 complex, and stabilizes actin filaments. Microinjection of WIP into NIH 3T3 fibroblasts induces filopodial this is inhibited by microinjection of anti-N-WASP antibody. Microinjection of anti-WIP antibody inhibits induction of filopodia by bradykinin, by an active Cdc42 mutant (Cdc42(V12)) and by N-WASP. Our results indicate that WIP and N-WASP may act as a functional unit in filopodium formation, which is consistent with their role in actin-tail formation in cells infected with vaccinia virus or Shigella.

引用

页码：484 / 491

页数：8

共 36 条

[1] The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck [J].