Cheng-Yuan Peng, Paul R. Graves, Richard S. Thoma, Zhiqi Wu, Andrey S. Shaw, Helen Piwnica-Worms
| Speaker: | 范丹琪 |
| Instructor: | 許宗雄老師 |
| Date: | 04/29/98 |
| Abstract: |
| Human Cdc25C is a protein phosphatase that dephosphorylates and activates Cdc2-cyclin B to trigger entry into mitosis. Cdc25C is itself regulated by phosphorylation. Throughout interphase Cdc25C was phosphorylated on serine-216 and bound to members of 14-3-3 family proteins. Mutaion of serine-216 abrogated binding of 14-3-3 to Cdc25C, demonstrating that Ser216 is essential for the interaction. Phosphorylation of Cdc25C on serine-216 throughout interphase appears negatively regulate Cdc25C. Chk1 is a fission yeast kinase involved in the DNA damage checkpoint response. Serine-216 phosphorylation by Chk1 and 14-3-3 binding sequester Cdc25C from functionally interacting with Cdc2. Chk1 as possibly regulates the interactions between 14-3-3 and Cdc25C during DNA damage check point response. |
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