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Originally published In Press as doi:10.1074/jbc.M102284200 on May 21, 2001

J. Biol. Chem., Vol. 276, Issue 29, 27090-27097, July 20, 2001
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Laminin-10/11 and Fibronectin Differentially Regulate Integrin- dependent Rho and Rac Activation via p130Cas-CrkII-DOCK180 Pathway*

Jianguo Gu, Yasuhiro Sumida, Noriko Sanzen, and Kiyotoshi SekiguchiDagger

From the Division of Protein Chemistry, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan

The alpha 5 chain-containing laminin isoforms, laminins-10 and -11 (laminin-10/11), are the major components of the basement membrane, having potent cell-adhesive activity. We examined the cell-adhesive and integrin-mediated signaling activities of laminin-10/11 in comparison to fibronectin, the best characterized extracellular adhesive ligand. We found that laminin-10/11 are more active than fibronectin in promoting cell migration and preferentially activate Rac, not Rho, via the p130Cas-CrkII-DOCK180 pathway. Cells adhering to fibronectin develop stress fibers and focal contacts, whereas cells adhering to laminin-10/11 do not, consistent with the high cell migration-promoting activity of laminin-10/11. Pull-down assays of GTP-loaded Rac and Rho demonstrated the preferential activation of Rac on laminin-10/11, in contrast to the activation of Rho on fibronectin. Activation of Rac by laminin-10/11 was associated with the phosphorylation of p130Cas and an increased formation of a p130Cas-CrkII-DOCK180 complex. Cell migration on laminin-10/11 was suppressed by the expression of either a dominant-negative Rac or CrkII mutants defective in p130Cas or DOCK180 binding. This is the first report demonstrating a distinct activation of Rho family GTPases resulting from adhesion to different extracellular ligands.

* This work was supported by Special Coordination Funds from the Science and Technology Agencies of Japan, grants-in-aid from the Ministry of Education, Science, Sports, and Culture of Japan, and the Uehara Memorial Foundation.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.

Dagger To whom correspondence should be addressed: Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-8617; Fax: 81-6-6879-8619; E-mail: sekiguch@protein.osaka-u.ac.jp.

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