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Science 6 October 1995:
Vol. 270. no. 5233, pp. 90 - 93
DOI: 10.1126/science.270.5233.90

Reports

Dephosphorylation of Cdk2 Thr by the Cyclin-Dependent Kinase-Interacting Phosphatase KAP in the Absence of Cyclin

Randy Y. C. Poon and Tony Hunter

The activation of cyclin-dependent kinases (CDKs) requires the phosphorylation of a conserved threonine (Thr in Cdk2) by CDK-activating kinase (CAK). Human KAP (also called Cdi1), a CDK-associated phosphatase, was shown to dephosphorylate Thr in human Cdk2. KAP was unable to dephosphorylate Tyr and only dephosphorylated Thr in native monomeric Cdk2. The binding of cyclin A to Cdk2 inhibited the dephosphorylation of Thr by KAP but did not preclude the binding of KAP to the cyclin A-Cdk2 complex. Moreover, the dephosphorylation of Thr by KAP prevented Cdk2 kinase activity upon subsequent association with cyclin A. These results suggest that KAP binds to Cdk2 and dephosphorylates Thr when the associated cyclin subunit is degraded or dissociates.


Molecular Biology and Virology Laboratory, Salk Institute for Biological Studies, 10100 North Torrey Pines Road, La Jolla, CA 92037-1099, USA.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)