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At mitotic entry, Plk1 phosphorylates and activates Cdc25C phosphatase, whereas it phosphorylates and down-regulates Wee1A. Plk1 also phosphorylates and inhibits Myt1 activity. Cyclin B1-bound Cdc2, which is the target of Cdc25C, Wee1A, and Myt1, functions in a feedback loop and phosphorylates the latter components (Cdc25C, Wee1A, Myt1). The Cdc2- dependent phosphorylation provides docking sites for the polo-box domain of Plk1, thus promoting the Plk1-dependent regulation of these components and, as a result, activation of Cdc2-Cyclin B1., Authored: Lee, KS, 2004-12-08 21:18:23, Edited: Gillespie, ME, 0000-00-00 00:00:00
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Polo-like kinase mediated events
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