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Mol Cell Biol, July 1998, p. 3659-3667, Vol. 18, No. 7
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases

Elizabeth A. Egan1 and Mark J. Solomon2 *

Department of Cell Biology1 and Department of Molecular Biophysics and Biochemistry,2 Yale University School of Medicine, New Haven, Connecticut 06520-8024

Received 10 October 1997/Returned for modification 18 November 1997/Accepted 25 March 1998

Although Cks proteins were the first identified binding partners of cyclin-dependent protein kinases (cdks), their cell cycle functions have remained unclear. To help elucidate the function of Cks proteins, we examined whether their binding to p34cdc2 (the mitotic cdk) varies during the cell cycle in Xenopus egg extracts. We observed that binding of human CksHs2 to p34cdc2 was stimulated by cyclin B. This stimulation was dependent on the activating phosphorylation of p34cdc2 on Thr-161, which follows cyclin binding and is mediated by the cdk-activating kinase. Neither the inhibitory phosphorylations of p34cdc2 nor the catalytic activity of p34cdc2 was required for this stimulation. Stimulated binding of CksHs2 to another cdk, p33cdk2, required both cyclin A and activating phosphorylation. Our findings support recent models that suggest that Cks proteins target active forms of p34cdc2 to substrates.

* Corresponding author. Mailing address: Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06520-8024. Phone: (203) 737-2702. Fax: (203) 785-6404. E-mail: Mark.Solomon{at}Yale.edu.

Mol Cell Biol, July 1998, p. 3659-3667, Vol. 18, No. 7
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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