Dephosphorylation of Cdk2 Thr160 by the Cyclin-Dependent Kinase-Interacting Phosphatase KAP in the Absence of Cyclin

@article{Poon1995DephosphorylationOC,
  title={Dephosphorylation of Cdk2 Thr160 by the Cyclin-Dependent Kinase-Interacting Phosphatase KAP in the Absence of Cyclin},
  author={R. Poon and T. Hunter},
  journal={Science},
  year={1995},
  volume={270},
  pages={90 - 93}
}
The activation of cyclin-dependent kinases (CDKs) requires the phosphorylation of a conserved threonine (Thr160 in Cdk2) by CDK-activating kinase (CAK). Human KAP (also called Cdi1), a CDK-associated phosphatase, was shown to dephosphorylate Thr160 in human Cdk2. KAP was unable to dephosphorylate Tyr15 and only dephosphorylated Thr160 in native monomeric Cdk2. The binding of cyclin A to Cdk2 inhibited the dephosphorylation of Thr160 by KAP but did not preclude the binding of KAP to the cyclin A… Expand
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