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Originally published In Press as doi:10.1074/jbc.M002942200 on June 22, 2000

J. Biol. Chem., Vol. 275, Issue 37, 28849-28857, September 15, 2000
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An Essential Phosphorylation-site Domain of Human cdc25C Interacts with Both 14-3-3 and Cyclins*

May C. MorrisDagger , Annie Heitz§, Jean Mery, Frederic Heitz, and Gilles DivitaDagger ||

From the Dagger  The Scripps Research Institute, Department of Molecular Biology, La Jolla, California 92037, § Center de Biochimie Structurale-CNRS (UMR 9955) and INSERM U 414, Faculté de Pharmacie, 15 Avenue Charles Flahault, 34060 Montpellier Cedex, France, and  Centre de Recherches de Biochimie Macromoléculaire, Biophysics unit, CNRS-UPR 1086, 1919 route de Mende, 34293 Montpellier Cedex 5, France

Human cdc25C is a dual-specificity phosphatase involved in the regulation of cell cycle progression in both unperturbed cells and in cells subject to DNA damage or replication checkpoints. In this study, we describe the structure-function relationship of an essential domain of human cdc25C that interacts with 14-3-3 proteins. We show that this domain is a bi-functional interactive motif that interacts with cyclins primarily through their P-box motif in addition to 14-3-3 proteins. Characterization of the structural features of this domain by NMR and circular dichroism reveals two distinct alpha  helical moieties interconnected by a loop carrying the 14-3-3 binding site. Moreover, the helical folding is induced upon binding to 14-3-3, suggestive of a conformational regulation of this domain of cdc25C through interactions with partner proteins in vivo. Combining our structural and biochemical data, we propose a detailed model of the molecular mechanism of cdc25C regulation by differential association with 14-3-3 and cdc2-cyclin B.

* This work was supported by grants from the CNRS, l'Association de Recherche Contre le Cancer, and La Ligue de Recherche contre Le Cancer (to G. D.).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: The Scripps Research Institute, Dept. of Molecular Biology, MB4, 10550 North Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-784-8065; Fax: 858-784-2277; E-mail: gilles@scripps.edu.

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