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Originally published In Press as doi:10.1074/jbc.M203457200 on April 18, 2002

J. Biol. Chem., Vol. 277, Issue 27, 24435-24441, July 5, 2002
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Calpain Cleaves RhoA Generating a Dominant-negative Form That Inhibits Integrin-induced Actin Filament Assembly and Cell Spreading*

Sucheta KulkarniDagger , Darrel E. Goll§, and Joan E. B. FoxDagger ||

From the Dagger  Department of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology, The Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, the § Muscle Biology Group, University of Arizona, Tucson, Arizona 85721, and the  Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106

Integrin-induced cell adhesion results in transmission of signals that induce cytoskeletal reorganizations and resulting changes in cell behavior. The cytoskeletal reorganizations are regulated by transient activation and inactivation of Rho GTPases. Previously, we identified µ-calpain as an enzyme that is activated by signaling across beta 1 and beta 3 integrins. We showed that it mediates cytoskeletal reorganizations in bovine aortic endothelial (BAE) and Chinese hamster ovary (CHO) cells and does so by acting upstream of Rac1 activation. Here we show that µ-calpain is also involved in inactivating RhoA during integrin-induced signaling. Cleavage of RhoA was detectable in BAE cells plated on an integrin substrate; it did not occur in cells plated on poly-L-lysine. Cleavage was inhibited by calpain inhibitors. In vitro, µ-calpain cleaved RhoA generating a fragment of the same size as in intact cells. The cleavage site was identified, an HA-tagged construct expressing calpain-cleaved RhoA generated, and the construct expressed in BAE and CHO cells. Calpain-cleaved RhoA inhibited integrin-induced stress fiber assembly and decreased cell spreading. Together, our data show that calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading.

* This work was supported by research grants HL30657 and HL56264 (to J. E. B. F.) from the National Institutes of Health.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.

|| To whom correspondence should be addressed: Joseph J. Jacobs Center for Thrombosis and Vascular Biology, (NB-50), The Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Ave., Cleveland, OH 44195. Tel.: 216-445-3874; Fax: 216-445-2051; E-mail: foxj@ccf.org.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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