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Vol. 9, Issue 2, 345-354, February 1998
Division of Biology, Howard Hughes Medical Institute, California
Institute of Technology, Pasadena, California 91125
Cdc25, the dual-specificity phosphatase that dephosphorylates the
Cdc2-cyclin B complex at mitosis, is highly regulated during the cell
cycle. In Xenopus egg extracts, Cdc25 is associated with two isoforms of the 14-3-3 protein. Cdc25 is complexed primarily with
14-3-3
and to a lesser extent with 14-3-3
. The association of
these 14-3-3 proteins with Cdc25 varies dramatically during the cell
cycle: binding is high during interphase but virtually absent at
mitosis. Interaction with 14-3-3 is mediated by phosphorylation of
Xenopus Cdc25 at Ser-287, which resides in a consensus
14-3-3 binding site. Recombinant Cdc25 with a point mutation at this residue (Cdc25-S287A) is incapable of binding to 14-3-3. Addition of
the Cdc25-S287A mutant to Xenopus egg extracts
accelerates mitosis and overrides checkpoint-mediated arrests of
mitotic entry due to the presence of unreplicated and damaged DNA.
These findings indicate that 14-3-3 proteins act as negative regulators
of Cdc25 in controlling the G2-M transition.
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