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Originally published In Press as doi:10.1074/jbc.M007541200 on November 30, 2000

J. Biol. Chem., Vol. 276, Issue 9, 6846-6852, March 2, 2001
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Regulation of Rac and Cdc42 Pathways by Gi during Lysophosphatidic Acid-induced Cell Spreading*

Hiroshi UedaDagger , Rika MorishitaDagger , Junji Yamauchi§, Hiroshi Itoh§||, Kanefusa KatoDagger , and Tomiko AsanoDagger **

From the Dagger  Department of Biochemistry, Institute for Developmental Research, Aichi Human Service Center, Kasugai, Aichi 480-0392 and the § Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan

The pertussis toxin-sensitive G protein, Gi, has been implicated in lysophosphatidic acid-induced cell mitogenesis and migration, but the mechanisms remain to be detailed. In the present study, we found that pertussis toxin blocks lysophosphatidic acid-induced cell spreading of NIH 3T3 fibroblasts on fibronectin. This prevention of cell spreading was eliminated by the expression of constitutively active mutants of Rho family small GTP-binding proteins, Rac and Cdc42, but not by Rho. In addition, activation of the endogenous forms was suppressed by pertussis toxin, indicating that Gi-induced cell spreading is mediated through the Rac and Cdc42 pathway. Transfection of constitutively active mutants of Galpha i and Galpha 11 and Gbeta gamma subunits enhanced spreading of pertussis toxin-treated cells. Gbeta 1 with Ggamma 12, a major Ggamma form in fibroblasts, was more effective for increasing cell spreading than Gbeta 1gamma 2 or Gbeta 1 plus Ggamma 12S2A, a mutant in which Ser-2, a phosphorylation site for protein kinase C, is replaced with alanine. In addition, a protein kinase C inhibitor diminished Gbeta 1gamma 12-induced cell spreading, suggesting a role for phosphorylation of the protein. These findings indicate that both Galpha i and Gbeta gamma stimulate Rac and Cdc42 pathways with lysophosphatidic acid-induced cell spreading on fibronectin.

* This work was supported in part by grants-in-aid for scientific research from the Ministry of Education, Science, Sports, and Culture of Japan, and by a grant from CREST of Japan Science and Technology.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Dept. of Molecular Cell Pharmacology, National Children's Medical Research Center, Tokyo 154-8509, Japan.

|| Present address: Graduate School of Agriculture and Life Science, University of Tokyo, Tokyo 113-8657, Japan.

** To whom correspondence should be addressed: Dept. of Biochemistry, Inst. for Developmental Research, Aichi Human Service Center, Kamiya-cho, Kasugai, Aichi 480-0392, Japan. Tel.: 81-568-88-0811; Fax: 81-568-88-0829; E-mail: toasano@inst-hsc.pref.aichi.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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