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Vol. 12, Issue 3, 551-563, March 2001
Division of Biology 216-76, Howard Hughes Medical Institute,
California Institute of Technology, Pasadena, California 91125
Wee1 inactivates the Cdc2-cyclin B complex during interphase by
phosphorylating Cdc2 on Tyr-15. The activity of Wee1 is highly regulated during the cell cycle. In frog egg extracts, it has been
established previously that Xenopus Wee1 (Xwee1) is
present in a hypophosphorylated, active form during interphase and
undergoes down-regulation by extensive phosphorylation at M-phase. We
report that Xwee1 is also regulated by association with 14-3-3 proteins. Binding of 14-3-3 to Xwee1 occurs during interphase, but not
M-phase, and requires phosphorylation of Xwee1 on Ser-549. A mutant of Xwee1 (S549A) that cannot bind 14-3-3 is substantially less active than
wild-type Xwee1 in its ability to phosphorylate Cdc2. This mutation
also affects the intranuclear distribution of Xwee1. In cell-free
kinase assays, Xchk1 phosphorylates Xwee1 on Ser-549. The results of
experiments in which Xwee1, Xchk1, or both were immunodepleted from
Xenopus egg extracts suggested that these two enzymes
are involved in a common pathway in the DNA replication checkpoint
response. Replacement of endogenous Xwee1 with recombinant Xwee1-S549A
in egg extracts attenuated the cell cycle delay induced by addition of
excess recombinant Xchk1. Taken together, these results suggest that
Xchk1 and 14-3-3 proteins act together as positive regulators of Xwee1.
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