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

Nature volume 378, pages 739–743 (1995)Cite this article

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.

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  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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