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Originally published In Press as doi:10.1074/jbc.M210628200 on December 8, 2002

J. Biol. Chem., Vol. 278, Issue 9, 6936-6941, February 28, 2003
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Characterization of a Novel Negative Regulator (DOC-2/DAB2) of c-Src in Normal Prostatic Epithelium and Cancer*

Jian Zhou, Jessica Scholes, and Jer-Tsong HsiehDagger

From the Department of Urology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9110

DOC-2/DAB2 is a potent tumor suppressor in many cancer types including prostate cancer. In prostate cancer, expression of DOC-2/DAB2 can inhibit its growth. Our recent studies demonstrate that DOC-2/DAB2 can suppress both protein kinase C and peptide growth factor-elicited signal pathways via the Ras-mitogen-activated protein kinase pathway. In this study, we further showed that the proline-rich domain of DOC-2/DAB2 could also interact with proteins containing the Src homology 3 domain, such as Src and Fgr. The binding of c-Src to DOC-2/DAB2 was enhanced in cells treated with growth factor, and this interaction resulted in c-Src inactivation. The c-Src inactivation was evidenced by the decreased tyrosine 416 phosphorylation of c-Src and reduced downstream effector activation. It appears that DOC-2/DAB2 can bind to Src homology 3 domain of c-Src and maintain it in an inactive conformation. Thus, this study provides a new mechanism for modulating c-Src in prostatic epithelium and cancer.

* This work was supported in part by National Institutes of Health Grant DK 47657 and by United States Army Grant PC970259.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: University of Texas Southwestern Medical Center, Department of Urology, 5323 Harry Hines Blvd., Dallas, TX 75390-9110. Tel.: 214-648-3988; Fax: 214-648-8786; E-mail: JT.Hsieh@UTSouthwestern.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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