Title : Successive phosphorylation of p27(KIP1) protein at serine-10 and C terminus crucially controls its potency to inactivate Cdk2.

Pub. Date : 2012 Jun 22

PMID : 22584582






3 Functional Relationships(s)
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1 Successive phosphorylation of p27(KIP1) protein at serine-10 and C terminus crucially controls its potency to inactivate Cdk2. Serine cyclin dependent kinase 2 Homo sapiens
2 During the G(1)-S transition, the activity of Cdk2 is regulated by its association with p27(KIP1), which in rodent fibroblasts undergoes phosphorylation mainly at serine 10, threonine 187, and C-terminal threonine 197 by KIS, Cdk2, and Pim or ROCK, respectively. Serine cyclin dependent kinase 2 Homo sapiens
3 We report here that serine 10 phosphorylation is required for efficient C-terminal phosphorylation of its own by PIM and ROCK kinases and critically controls the potency of p27 as a Cdk2 inhibitor. Serine cyclin dependent kinase 2 Homo sapiens