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Vol. 9, Issue 12, 3321-3334, December 1998
Departments of Molecular Biology and Cell Biology, The Scripps
Research Institute, La Jolla, California 92037
Cdc2-Cyclin B, the protein kinase that catalyzes the onset of
mitosis, is subject to multiple forms of regulation. In the fission
yeast Schizosaccharomyces pombe and most other species, a key mode of Cdc2-Cyclin B regulation is the inhibitory
phosphorylation of Cdc2 on tyrosine-15. This phosphorylation is
catalyzed by the protein kinases Wee1 and Mik1 and removed by the
phosphatase Cdc25. These proteins are also regulated, a notable example
being the inhibition of Wee1 by the protein kinase Nim1/Cdr1. The
temperature-sensitive mutation cdc25-22 is synthetic
lethal with nim1/cdr1 mutations, suggesting that a
synthetic lethal genetic screen could be used to identify novel mitotic
regulators. Here we describe that such a screen has identified
cdr2+, a gene that has an important role in
the mitotic control. Cdr2 is a 775 amino acid protein kinase that is
closely related to Nim1 and mitotic control proteins in budding yeast.
Deletion of cdr2 causes a G2-M delay that is more severe
than that caused by nim1/cdr1 mutations.
Genetic studies are consistent with a model in which Cdr2 negatively
regulates Wee1. This model is supported by experiments showing that
Cdr2 associates with the N-terminal regulatory domain of Wee1 in cell
lysates and phosphorylates Wee1 in vitro. Thus, Cdr2 is a novel mitotic
control protein that appears to regulate Wee1.
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