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Fission yeast Clp1p phosphatase affects G 2 /M transition and mitotic exit through Cdc25p inactivation
Author(s) -
Wolfe Benjamin A,
Gould Kathleen L
Publication year - 2004
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600103
Subject(s) - biology , yeast , mitosis , microbiology and biotechnology , phosphatase , fission , schizosaccharomyces , mitotic exit , transition (genetics) , genetics , saccharomyces cerevisiae , schizosaccharomyces pombe , cell division , cell , spindle apparatus , gene , phosphorylation , physics , quantum mechanics , neutron
The Cdc14 family of phosphatases specifically reverses proline‐directed phosphorylation events. In Saccharomyces cerevisiae , Cdc14p promotes Cdk1p inactivation at mitotic exit by reversing Cdk1p‐dependent phosphorylations. Cdk1p is a proline‐directed kinase whose activity is required in all eukaryotes for the transit into mitosis. At mitotic commitment, Cdk1p participates in its own regulation by activating the mitotic inducing phosphatase, Cdc25p, and inhibiting the opposing kinase, Wee1p. We have investigated the ability of Schizosaccharomyces pombe Clp1p, a Cdc14p homolog, to disrupt this auto‐amplification loop. We show here that Clp1p is required to dephosphorylate, destabilize, and inactivate Cdc25p at the end of mitosis. Clp1p promotes recognition of Cdc25p by the anaphase‐promoting complex/cyclosome, an E3 ubiquitin ligase. Failure to inactivate and destabilize Cdc25p in late mitosis delays progression through anaphase, interferes with septation initiation network signaling, and additionally advances the commitment to mitotic entry in the next cycle. This may be a widely conserved mechanism whereby Cdc14 proteins contribute to Cdk1p inactivation.