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Originally published In Press as doi:10.1074/jbc.M201178200 on June 13, 2002

J. Biol. Chem., Vol. 277, Issue 35, 31938-31948, August 30, 2002
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Involvement of Cell-Cell Interactions in the Rapid Stimulation of Cas Tyrosine Phosphorylation and Src Kinase Activity by Transforming Growth Factor-beta 1*

Jong-Tak Kim and Choun-Ki JooDagger

From the Laboratory of Visual Science, College of Medicine, The Catholic University of Korea, and Catholic Research Institutes of Medical Science, Seoul 137 040, Korea

Transforming growth factor-beta (TGF-beta ) regulates a wide range of physiological and pathological cellular processes, including cell migration, mesenchymal transition, extracellular matrix synthesis, and cell death. Cas (Crk-associated substrate, 130 kDa), an adaptor protein localized at focal adhesions and stress fibers, is also known to have important functions in cell migration and the induction of immediate-early gene expression. Here, we report that a rapid and transient tyrosine phosphorylation of Cas is induced by TGF-beta 1 and that E-cadherin-mediated cell-cell interaction and the Src kinase pathway are involved in this early TGF-beta signaling. The addition of TGF-beta 1 to epithelial cells rapidly induced tyrosine phosphorylation of Cas and promoted the formation of complexes between focal adhesion molecules. Cas phosphorylation required the integrity of the actin cytoskeleton but was not dependent on cell adhesion, implying that Cas-dependent signaling may be distinct from integrin signaling. TGF-beta 1 also stimulated Src kinase activity, and specific inhibitors of Src completely blocked the induction of Cas phosphorylation by TGF-beta 1. The Cas phosphorylation and Src kinase activation seen in our results were induced in an epithelial phenotype-specific manner. Stable transfection of E-cadherin to L929 cells and L cells as well as E-cadherin blocking assay revealed that E-cadherin-mediated cell-cell interactions were essential for both Cas phosphorylation and Src kinase activation. Taken together, our data suggest that rapid Cas phosphorylation and Src kinase activation may play a novel role in TGF-beta signal transduction.

* This work was supported by Grant 00-J-LF-01-B-78 from the Korea Ministry of Science and Technology (Critical Technology 21 on "Life Phenomena and Function Research").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: Laboratory of Ophthalmology and Visual Science, College of Medicine, The Catholic University of Korea, 505 Banpo-dong, Seocho-ku, Seoul, Korea. Tel.: 82-2-590-2613; Fax: 82-2-533-3801; E-mail: ckjoo@catholic.ac.kr.

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