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Cdk1, also known as p34 [cdc2], is a ubiquitously expressed serine/threonine protein kinase. Cdk1/cdc2 has been identified as the catalytic subunit of the maturation-promoting factor (MPF), while cyclin B acts as the regulatory subunit. The binding of these two subunits is critical to the transition into M-phase of the mammalian cell cycle, and this factor's role is regulated by a series of phosphorylations and dephosphorylations. After binding to cyclin B, cdk1/cdc2 is phosphorylated on Thr-14, by Myt1, and Tyr-15, by wee1 or mik1, yielding an inactive pre-MPF complex. Phosphorylation of cdk1/cdc2 on Thr-161 is performed by a cdk7/cyclin H complex and is necessary for activation of the cdc2 complex. Dephosphorylation of Thr-14 and Tyr-15 by CDC25 occurs at the prophase/metaphase transition and completes activation of the cdc2/cyclin B complex, initiating the cell's entry into mitosis.
