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

Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases Elizabeth A. Egan 1 and Mark J. Solomon 2 , * Department of Cell Biology 1 and Department of Molecular Biophysics and Biochemistry, 2 Yale University School of Medicine, New Haven, Connecticut 06520-8024 ABSTRACT 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 p34 cdc2 (the mitotic cdk) varies during the cell cycle in Xenopus egg extracts. We observed that binding of human CksHs2 to p34 cdc2 was stimulated by cyclin B. This stimulation was dependent on the activating phosphorylation of p34 cdc2 on Thr-161, which follows cyclin binding and is mediated by the cdk-activating kinase. Neither the inhibitory phosphorylations of p34 cdc2 nor the catalytic activity of p34 cdc2 was required for this stimulation. Stimulated binding of CksHs2 to another cdk, p33 cdk2 , required both cyclin A and activating phosphorylation. Our findings support recent models that suggest that Cks proteins target active forms of p34 cdc2 to substrates. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular and Cellular Biology American Society For Microbiology

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

Molecular and Cellular Biology , Volume 18 (7): 3659 – Jul 1, 1998

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

Molecular and Cellular Biology , Volume 18 (7): 3659 – Jul 1, 1998

Abstract

Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases Elizabeth A. Egan 1 and Mark J. Solomon 2 , * Department of Cell Biology 1 and Department of Molecular Biophysics and Biochemistry, 2 Yale University School of Medicine, New Haven, Connecticut 06520-8024 ABSTRACT 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 p34 cdc2 (the mitotic cdk) varies during the cell cycle in Xenopus egg extracts. We observed that binding of human CksHs2 to p34 cdc2 was stimulated by cyclin B. This stimulation was dependent on the activating phosphorylation of p34 cdc2 on Thr-161, which follows cyclin binding and is mediated by the cdk-activating kinase. Neither the inhibitory phosphorylations of p34 cdc2 nor the catalytic activity of p34 cdc2 was required for this stimulation. Stimulated binding of CksHs2 to another cdk, p33 cdk2 , required both cyclin A and activating phosphorylation. Our findings support recent models that suggest that Cks proteins target active forms of p34 cdc2 to substrates.

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Publisher
American Society For Microbiology
Copyright
Copyright © 1998 by the American society for Microbiology.
ISSN
0270-7306
eISSN
1098-5549
Publisher site
See Article on Publisher Site

Abstract

Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases Elizabeth A. Egan 1 and Mark J. Solomon 2 , * Department of Cell Biology 1 and Department of Molecular Biophysics and Biochemistry, 2 Yale University School of Medicine, New Haven, Connecticut 06520-8024 ABSTRACT 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 p34 cdc2 (the mitotic cdk) varies during the cell cycle in Xenopus egg extracts. We observed that binding of human CksHs2 to p34 cdc2 was stimulated by cyclin B. This stimulation was dependent on the activating phosphorylation of p34 cdc2 on Thr-161, which follows cyclin binding and is mediated by the cdk-activating kinase. Neither the inhibitory phosphorylations of p34 cdc2 nor the catalytic activity of p34 cdc2 was required for this stimulation. Stimulated binding of CksHs2 to another cdk, p33 cdk2 , required both cyclin A and activating phosphorylation. Our findings support recent models that suggest that Cks proteins target active forms of p34 cdc2 to substrates.

Journal

Molecular and Cellular BiologyAmerican Society For Microbiology

Published: Jul 1, 1998

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