Multisite phosphoregulation of Cdc25 activity refines the mitotic entrance and exit switches.

@article{Lu2012MultisitePO,
  title={Multisite phosphoregulation of Cdc25 activity refines the mitotic entrance and exit switches.},
  author={Lucy X. Lu and Maria Rosa Domingo-Sananes and Malwina A. Huzarska and B{\'e}la Nov{\'a}k and Kathleen L. Gould},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 25},
  pages={9899-904}
}
Cyclin-dependent kinase 1 (Cdk1) kinase dephosphorylation and activation by Cdc25 phosphatase are essential for mitotic entry. Activated Cdk1 phosphorylates Cdc25 and other substrates, further activating Cdc25 to form a positive feedback loop that drives the abrupt G2/mitosis switch. Conversely, mitotic exit requires Cdk1 inactivation and reversal of Cdk1 substrate phosphorylation. This dephosphorylation is mediated, in part, by Clp1/Cdc14, a Cdk1-antagonizing phosphatase, which reverses Cdk1… CONTINUE READING
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