Phosphorylation and inactivation of the mitotic inhibitor Weel by the nim1/cdr1 kinase

@article{Parker1993PhosphorylationAI,
  title={Phosphorylation and inactivation of the mitotic inhibitor Weel by the nim1/cdr1 kinase},
  author={Laura L. Parker and Sarah A. Walter and Paul G. Young and Helen Piwnica-Worms},
  journal={Nature},
  year={1993},
  volume={363},
  pages={736-738}
}
THE G2-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 Cdc2, a serine/threonine protein kinase required for entry into mitosis (reviewed in ref. 1). In the fission yeast Schizosaccharomyces pombe, inactivation of the Cdc2/cyclin B complex is achieved by phosphorylation of tyrosine 15 by Weel (refs 2, 3). The action of the Weel kinase is opposed by the action of the Cdc25… CONTINUE READING

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