Abstract
Human Cdc25C is a protein phosphatase that dephosphorylates and activates Cdc2-cyclin B to trigger entry into mitosis. Cdc25C is itself regulated by phosphorylation. In asynchronously growing HeLa cells, we have determined that serine 216 is the major site of Cdc25C phosphorylation. We have isolated a protein kinase that binds to Cdc25C and phosphorylates serine 216. The kinase binds within amino acids 200-256 of Cdc25C. This region is conserved in some Cdc25 homologues and contains a putative bipartite nuclear localization signal just downstream from serine 216. Finally, the Cdc25C-associating kinase was purified over 8000-fold from rat liver as a 36-38-kDa doublet of proteins.
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