Targets of the cyclin-dependent kinase Cdk1

Jeffrey A. Ubersax, Erika L. Woodbury, Phuong N. Quang, Maria Paraz, Justin D. Blethrow, Kavita Shah, Kevan M. Shokat and David O. Morgan ()
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Jeffrey A. Ubersax: University of California
Erika L. Woodbury: University of California
Phuong N. Quang: University of California
Maria Paraz: University of California
Justin D. Blethrow: University of California
Kavita Shah: Genomics Institute of the Novartis Foundation
Kevan M. Shokat: University of California
David O. Morgan: University of California

Nature, 2003, vol. 425, issue 6960, 859-864

Abstract: Abstract The events of cell reproduction are governed by oscillations in the activities of cyclin-dependent kinases (Cdks)1. Cdks control the cell cycle by catalysing the transfer of phosphate from ATP to specific protein substrates. Despite their importance in cell-cycle control, few Cdk substrates have been identified2. Here, we screened a budding yeast proteomic library for proteins that are directly phosphorylated by Cdk1 in whole-cell extracts. We identified about 200 Cdk1 substrates, several of which are phosphorylated in vivo in a Cdk1-dependent manner. The identities of these substrates reveal that Cdk1 employs a global regulatory strategy involving phosphorylation of other regulatory molecules as well as phosphorylation of the molecular machines that drive cell-cycle events. Detailed analysis of these substrates is likely to yield important insights into cell-cycle regulation.

Date: 2003
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DOI: 10.1038/nature02062

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