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Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast

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Abstract

IN fission yeast the onset of mitosis is brought about by Cdc2/ Cdcl3 kinase, which is inhibited by the Weel/Mikl tyrosine kin-ases and activated by Cdc25 tyrosine phosphatase1. This control network integrates many signals, including those that monitor DNA replication, DNA damage and cell size. We report here that a fission yeast MAP kinase pathway links the cell-cycle G2/M control with changes in the extracellular environment that affect cell physiology. Fission yeast spc1 mutants have a G2 delay that is greatly exacerbated by growth in high osmolarity media and nutrient limitation. A lethal interaction of spc1 and cdc25 mutations shows that Spcl promotes the onset of mitosis. Spcl is a MAP kinase homologue that is activated by Wisl kinase in response to osmotic stress and nutrient limitation. Spcl is inactivated by Pypl, a phosphatase previously identified as a mitotic inhibitor2,3. Pypl dephosphorylates only tyrosine-173 of Spcl, unlike the dual-specificity phosphatases that have been shown to regulate other MAP kinases4.

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  1. Paul Russell: To whom correspondence should be addressed.

Authors and Affiliations

  1. Departments of Molecular Biology and Cell Biology, The Scripps Research Institute, La Jolla, California, 92037, USA

    Kazuhiro Shiozaki & Paul Russell

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  1. Kazuhiro Shiozaki
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  2. Paul Russell
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Shiozaki, K., Russell, P. Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast. Nature 378, 739–743 (1995). https://doi.org/10.1038/378739a0

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  • DOI: https://doi.org/10.1038/378739a0

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