Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1940870 | Biochemical and Biophysical Research Communications | 2006 | 10 Pages |
Abstract
Cyclin-dependent kinase 2 (Cdk2) activity is thought to be involved in cell death-associated chromatin condensation and other manifestations of apoptotic death. Here we show that during TNFα-induced apoptosis, PKCδ is activated in a caspase-3-dependent manner and phosphorylates p21WAF1/CIP1, a specific cyclin-dependent kinase inhibitor, on 146Ser. This residue is located near a cyclin-binding motif (Cy2) that plays an important role in the interaction between p21WAF1/CIP1 and Cdk2, and its phosphorylation modulates the ability of p21WAF1/CIP1 to associate with Cdk2. The phosphorylation of p21WAF1/CIP1 is temporally related to the activation kinetics of Cdk2 activity during the apoptosis. We propose that during TNFα-induced apoptosis, PKCδ-mediated phosphorylation of p21WAF1/CIP1 at 146Ser attenuates the Cdk2 binding of p21WAF1/CIP1 and thereby upregulates Cdk2 activity.
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Authors
You-Take Oh, Kwang Hoon Chun, Jeong In Oh, Jeong Ae Park, Yong Ung Kim, Seung Ki Lee,