Abstract
Cmk2, a fission yeast Ser/Thr protein kinase homologous to mammalian calmodulin kinases, is essential for oxidative stress response. Cells lacking cmk2 gene were specifically sensitive to oxidative stress conditions. Upon stress, Cmk2 was phosphorylated in vivo, and this phosphorylation was dependent on the stress-activated MAPK Sty1/Spc1. Co-precipitation assays demonstrated that Cmk2 binds Sty1. Furthermore, in vivo or in vitro activated Sty1 was able to phosphorylate Cmk2, and the phosphorylation occurred at the C-terminal regulatory domain at Thr-411. Cell lethality caused by overexpression of Wis1 MAPK kinase was abolished by deletion of cmk2 or by mutation of Thr-411 of Cmk2. Taken together, our data suggest that Cmk2 acts downstream of Sty1 and is an essential kinase for oxidative stress responses.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Mitogen-Activated Protein Kinase Kinases / metabolism
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Mitogen-Activated Protein Kinases / metabolism
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Molecular Sequence Data
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Oxidative Stress*
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Phosphorylation
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Point Mutation
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism
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Protein Serine-Threonine Kinases / physiology*
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Saccharomyces cerevisiae Proteins*
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Schizosaccharomyces / enzymology
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Schizosaccharomyces / physiology*
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Schizosaccharomyces pombe Proteins*
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Sequence Homology, Amino Acid
Substances
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Saccharomyces cerevisiae Proteins
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Schizosaccharomyces pombe Proteins
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Cmk2 protein, S pombe
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RCK2 protein, S cerevisiae
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Protein Serine-Threonine Kinases
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HOG1 protein, S cerevisiae
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Mitogen-Activated Protein Kinases
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sty1 protein, S pombe
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Mitogen-Activated Protein Kinase Kinases
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wis1 protein, S pombe