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XB-ART-13111
Cell April 16, 1999; 97 (2): 221-31.

The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly.

Rohatgi R , Ma L , Miki H , Lopez M , Kirchhausen T , Takenawa T , Kirschner MW .


Abstract
Although small GTP-binding proteins of the Rho family have been implicated in signaling to the actin cytoskeleton, the exact nature of the linkage has remained obscure. We describe a novel mechanism that links one Rho family member, Cdc42, to actin polymerization. N-WASP, a ubiquitously expressed Cdc42-interacting protein, is required for Cdc42-stimulated actin polymerization in Xenopus egg extracts. The C terminus of N-WASP binds to the Arp2/3 complex and dramatically stimulates its ability to nucleate actin polymerization. Although full-length N-WASP is less effective, its activity can be greatly enhanced by Cdc42 and phosphatidylinositol (4,5) bisphosphate. Therefore, N-WASP and the Arp2/3 complex comprise a core mechanism that directly connects signal transduction pathways to the stimulation of actin polymerization.

PubMed ID: 10219243
Article link: Cell
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: actl6a actr2 aicda cdc42 rho was wasl