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