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Alberts B, Johnson A, Lewis J, et al. Molecular Biology of the Cell. 4th edition. New York: Garland Science; 2002.
Cdk1 associates with M-cyclin as the levels of M-cyclin gradually rise. The resulting M-Cdk complex is phosphorylated on an activating site by the Cdk-activating kinase (CAK) and on a pair of inhibitory sites by the Wee1 kinase. The resulting inactive M-Cdk complex is then activated at the end of G2 by the phosphatase Cdc25. Cdc25 is stimulated in part by Polo kinase, which is not shown for simplicity. Cdc25 is further stimulated by active M-Cdk, resulting in positive feedback. This feedback is enhanced by the ability of M-Cdk to inhibit WeeI.
From: Intracellular Control of Cell-Cycle Events
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