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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© The Rockefeller University Press, 0021-9525/1998//1125 $5.00
The Journal of Cell Biology, Volume 140, Number 5, , 1998 1125-1136

Article

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 theRho 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 these pathways. We have found that GTP ${gamma}$ S stimulates actin assemblyin the presence of endogenous membrane vesicles in low speedextracts. These membrane vesicles are required, but can bereplaced by lipid vesicles prepared from purified phospholipidscontaining phosphoinositides. Vesicles containing phosphatidylinositol(4,5) bisphosphate or phosphatidylinositol (3,4,5) trisphosphatecan induce actin assembly even in the absence of GTP ${gamma}$ S. RhoGDI,a guanine-nucleotide dissociation inhibitor for the Rho family,inhibits phosphoinositide-induced actin assembly, suggestingthe involvement of the Rho family small G proteins. Using variousdominant mutants of these G proteins, we demonstrate the requirementof Cdc42 for phosphoinositide-induced actin assembly. Our resultssuggest that phosphoinositides may act to facilitate GTP exchange on Cdc42, as well as to anchor Cdc42 and actin nucleation activities.Hence, both phosphoinositides and Cdc42 are required to induceactin assembly in this cell-free system.

Abbreviations used in this paper: F-actin, filamentous actin; G proteins, GTP-binding proteins, GDI, guanine-nucleotide dissociation inhibitor; GEF, guanine-nucleotide exchange factor; NBD, nitrobenzoxadiazole; PC, phosphatidylcholine; PI, phosphatidyinositol; PI(4,5)P₂, PI (4,5) bisphosphate; PI(3,4)P₂, PI (3,4) bisphosphate; PI(3,4,5)P₃, PI (3,4,5) trisphosphate.

Address all correspondence to Marc Kirschner, Department ofCell Biology, Harvard Medical School, 240 Longwood Avenue, Boston,MA 02115. Tel.: 617-432-2250; Fax: 617-432-0420. E-mail: marc{at}hms.harvard.edu

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