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Originally published In Press as doi:10.1074/jbc.M001818200 on August 22, 2000

J. Biol. Chem., Vol. 275, Issue 47, 37219-37223, November 24, 2000
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Integrin Engagement, the Actin Cytoskeleton, and c-Src Are Required for the Calcitonin-induced Tyrosine Phosphorylation of Paxillin and HEF1, but Not for Calcitonin-induced Erk1/2 Phosphorylation*

Zhiyuan Zhang, Roland Baron, and William C. HorneDagger

From the Departments of Cell Biology and Orthopaedics and the Yale Cancer Center, Yale University School of Medicine, New Haven, Connecticut 06520-8044

We have previously shown that in a HEK-293 cell line that overexpresses the C1a isoform of the calcitonin receptor (C1a-HEK), calcitonin induces the tyrosine phosphorylation of the focal adhesion-associated proteins HEF1 (a p130Cas-like docking protein), paxillin, and focal adhesion kinase and that it also stimulates the phosphorylation and activation of Erk1 and Erk2. We report here that cell attachment to the extracellular matrix, an intact actin cytoskeleton, and c-Src are absolutely required for the calcitonin-induced phosphorylation of focal adhesion-associated proteins. In contrast to the phosphorylation of paxillin and HEF1 in cells attached to fibronectin-coated dishes, calcitonin failed to stimulate the phosphorylation of paxillin and HEF1 in suspended cells, in cells attached to poly-D-lysine-coated dishes, and in attached cells pretreated with the RGD-containing peptide GRGDS. Overexpression of wild-type c-Src increased calcitonin-induced paxillin and HEF1 phosphorylation, whereas overexpression of kinase-dead Src or Src lacking a functional SH2 domain inhibited the calcitonin-stimulated tyrosine phosphorylation of these proteins. Overexpression of Src lacking the SH3 domain did not affect the calcitonin-induced phosphorylation of paxillin and HEF1. In contrast to the regulation of paxillin and HEF1 phosphorylation, the calcitonin-induced phosphorylation of Erk1 and Erk2 did not appear to involve c-Src and was only partially dependent on cell adhesion to the extracellular matrix and an intact actin cytoskeleton. Furthermore, inhibition of Erk1 and Erk2 phosphorylation had no effect on the calcitonin-induced phosphorylation of paxillin and HEF1. Thus, in C1a-HEK cells, the calcitonin receptor is coupled to the tyrosine phosphorylation of focal adhesion-associated proteins and to Erk1/2 phosphorylation by mechanisms that are in large part independent.

* This work was supported by National Institutes of Health Grants DE-04724 and AR-42927 (to R. B.) and by Yale Core Center for Musculoskeletal Disorders Grant AR-46032 (to W. C. H.).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: Dept. of Orthopaedics, Yale University School of Medicine, P. O. Box 208044, New Haven, CT 06520-8044. Tel.: 203-785-2165; Fax: 203-785-2744; E-mail: william.horne@yale.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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