Corequirement of Specific Phosphoinositides and Small GTP-binding Protein Cdc42 in Inducing Actin Assembly in Xenopus Egg Extracts

doi:10.1083/jcb.140.5.1125

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J. Cell Biol., Volume 140, Number 5, March 9, 1998 1125-1136

Corequirement of Specific Phosphoinositides and Small GTP-binding Protein Cdc42 in Inducing Actin Assembly in Xenopus Egg Extracts

Le Ma,^* Lewis C. Cantley,^* Paul A. Janmey,^§ and Marc W. Kirschner^*

^* Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115; Division of Signal Transduction, Beth Israel Hospital, Boston, Massachusetts 02115; and ^§ Division of Experimental Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115

Both phosphoinositides and small GTP-binding proteins of the Rho family have been postulated to regulate actin assembly incells. We have reconstituted actin assembly in response to thesesignals in Xenopus extracts and examined the relationship of thesepathways. We have found that GTP $gamma$ S stimulates actin assembly inthe presence of endogenous membrane vesicles in low speed extracts.These membrane vesicles are required, but can be replaced by lipidvesicles prepared from purified phospholipids containing phosphoinositides.Vesicles containing phosphatidylinositol (4,5) bisphosphate orphosphatidylinositol (3,4,5) trisphosphate can induce actin assemblyeven in the absence of GTP $gamma$ S. RhoGDI, a guanine-nucleotide dissociationinhibitor for the Rho family, inhibits phosphoinositide-inducedactin assembly, suggesting the involvement of the Rho family smallG proteins. Using various dominant mutants of these G proteins,we demonstrate the requirement of Cdc42 for phosphoinositide-inducedactin assembly. Our results suggest that phosphoinositides mayact to facilitate GTP exchange on Cdc42, as well as to anchorCdc42 and actin nucleation activities. Hence, both phosphoinositidesand Cdc42 are required to induce actin assembly in this cell-freesystem.

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