Abstract
The G2 to M phase transition in eukaryotes is regulated by the synergistic and opposing activities of a cascade of distinct protein kinases and phosphatases. This cascade converges on p34cdc2, a serine/threonine protein kinase that regulates entry into mitosis (reviewed in 1). The kinase activity of p34cdc2 is stimulated both by its association with cyclin B and by its phosphorylation on threonine 161 2–11. In Schizosaccharomyces pombe, inactivation of the p34cdc2/cyelin B complex occurs by phosphorylation of tyrosine 15 by pl07wee1 8, 12. In human cells, p34cdc2/cyelin B kinase activity is negatively regulated by phosphorylation on tyrosine 15 (by p49WEEIHu, the human homolog of pl07weel 13) and on threonine 14 14, 15. The action of the wee 1 kinase is opposed by the action of the cdc25 phosphatase. Cdc25 dephosphorylates p34cdc2 on tyrosine 15 and on threonine 14 resulting in the activation of the p34cdc2/cyclin Bcomplex 16–21.
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Parker, L.L., Walter, S.A., Piwnica-Worms, H. (1994). Direct Inhibition of p107WEE1 by the Nim 1/CDR 1 Kinase. In: Hu, V.W. (eds) The Cell Cycle. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2421-2_20
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DOI: https://doi.org/10.1007/978-1-4615-2421-2_20
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