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. 1999 Apr 16;97(2):221-31.
doi: 10.1016/s0092-8674(00)80732-1.

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

R Rohatgi  1 , L Ma, H Miki, M Lopez, T Kirchhausen, T Takenawa, M W Kirschner
Affiliations
Free article

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

R Rohatgi et al. Cell. .
Free article

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.

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