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===under info was translated buy computer===
Activation of cyclin-dependent kinases in higher eukaryotic cells can be achieved through dephosphorylation of two conserved residues, Thr14 and Tyr15 by members of the Cdc25 phosphatase family, Cdc25A, Cdc25B and Cdc25C. The Cdc25 dual-specificity phosphatases control progression through the eukaryotic cell division cycle by activating cyclin-dependent kinases. Cdc25A plays an important role at the G1/S-phase transition. Cdc25A degradation during mitotic exit and in early G1 is mediated by the anaphase-promoting complex or cyclosome (APC/C)(Cdh1) ligase, and that a KEN-box motif in the N-terminus of the protein is required for its targeted degradation. Cdc25B undergoes activation during S-phase and plays a role in activating the mitotic kinase Cdk1/cyclin B in the cytoplasm. Active Cdk1/cyclin B then phosphorylates and activates Cdc25C leading to a positive feedback mechanism and to entry into mitosis. In addition to their essential function in the normal cell cycle, cdc25 phosphatases are involved in the checkpoint-induced control of cell cycle progression. Finally, Cdc25A and B phosphatases have been shown to possess an important oncogenic potential and to be overexpressed in a variety of cancers and cancer cell lines.
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