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Cdc25
Cdc25 is a dual-specificity phosphatase first isolated from the yeast ''Schizosaccharomyces pombe'' as a cell cycle defective mutant. As with other cell cycle proteins such as Cdc2 and Cdc4, the "cdc" in its name refers to "cell division cycle".
Dual-specificity phosphatases are considered a sub-class of protein tyrosine phosphatases. By removing inhibitory phosphate residues from target Cyclin-Dependent Kinases (Cdks), Cdc25 proteins control entry into and progression through various phases of the cell cycle, including mitosis and S ("Synthesis") phase.
==Function of Cdc25 in Activating Cdk1==
Cdc25 activates cyclin dependent kinases by removing phosphate from residues in the Cdk active site. Also, the phosphorylation of M-Cdk (a complex of Cdk1 and cyclin B) activates Cdc25. Together with Wee1, M-Cdk activation is switch-like. The switch-like behavior forces entry into mitosis to be quick and irreversible. Cdk activity can be reactivated after dephosphorylation by Cdc25. The Cdc25 enzymes Cdc25A-C are known to control the transitions from G1 to S phase and G2 to M phase.〔Morgan, David. The Cell Cycle: Principles of Control. London: New Science Press, 2007. 96-98, 34-35. Print.〕
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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