The Cdc2/cyclin B enzyme, involved in regulation of mitosis in eukaryotic cells, is subject to multiple levels of control. Among these, the regulation of the catalytic subunit by Tyrosine phosphorylation is the best understood. Tyrosine phosphorylation inhibits the Cdc2/cyclin B complex, while Tyrosine dephosphorylation, which occurs at the onset of mitosis, directly activates the pre-MPH complex. The Cdc25 gene serves as a rate-limiting mitotic activator, apparently due to its action as the Cdc2 Tyrosine phosphatase. In the absence of Cdc25, Cdc2 accumulates in a Tyrosine phosphorylated state. In addition, Cdc25 proteins from a variety of species have been shown to share a low degree of sequence similarity with other Tyrosine phosphatases. The Cdc25 gene family consists of at least three members that share approximately 40% identity in their most conserved carboxy-terminal sequences.
