Volume 272, Number 52, Issue of December 26, 1997 pp. 32731-32734

COMMUNICATION:
Phosphorylation of Human CDC25B Phosphatase by CDK1-Cyclin A Triggers Its Proteasome-dependent Degradation

(Received for publication, October 10, 1997, and in revised form, October 29, 1997)

From the Institut de Pharmacologie et de Biologie Structurale du CNRS, Université Paul Sabatier, 205 route de Narbonne, 31077 Toulouse cedex, France

In eukaryotes the activity of CDK1 (CDC2), a cyclin-dependent kinase that initiates the structural changes that culminate in the segregation of chromosomes at mitosis, is regulated by the synergistic and opposing activities of a cascade of kinases and phosphatases. Dephosphorylation of threonine 14 and tyrosine 15 of CDK1 by the CDC25 phosphatases is a key step in the activation of the CDK1-cyclin B protein kinase. Little is currently known about the role and the regulation of CDC25B. Here we report in vitro and in vivo data that indicate that CDC25B is degraded by the proteasome. This degradation is dependent upon phosphorylation by the CDK1-cyclin A complex but not by CDK1-cyclin B. These results indicate that CDK1-cyclin A phosphorylation targets CDC25B for degradation and that this might be an important component of cell cycle regulation at the G₂/M transition.

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