Multiple modes of activation of the stress-responsive MAP kinase pathway in fission yeast
The Schizosaccharomyces pombe wis1+ gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of the MAPK homologue Spc1, and integrity of the Wis1–Spc1 pathway is required for survival in extreme conditions of heat, osmolarity, oxidation or lim...
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| Published in | The EMBO journal Vol. 16; no. 20; pp. 6162 - 6170 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
15.10.1997
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| Abstract | The Schizosaccharomyces pombe wis1+ gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of the MAPK homologue Spc1, and integrity of the Wis1–Spc1 pathway is required for survival in extreme conditions of heat, osmolarity, oxidation or limited nutrition. We show here that Wis4, a protein kinase of a new MAPKKK class, phosphorylates Wis1 in vitro and activates it in vivo. Win1 is also required for full activation of Wis1, and Win1 rather than Wis4 mediates the osmotic stress signal. Surprisingly, the pathway can still be activated by heat or oxidative stress independently of the phosphorylation of two conserved Wis1 residues. Evidence is presented that the Pyp1 protein tyrosine phosphatase, which dephosphorylates Spc1, is central to this alternative activation mechanism. |
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| AbstractList | The Schizosaccharomyces pombe wis1(+) gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of the MAPK homologue Spc1, and integrity of the Wis1-Spc1 pathway is required for survival in extreme conditions of heat, osmolarity, oxidation or limited nutrition. We show here that Wis4, a protein kinase of a new MAPKKK class, phosphorylates Wis1 in vitro and activates it in vivo. Win1 is also required for full activation of Wis1, and Win1 rather than Wis4 mediates the osmotic stress signal. Surprisingly, the pathway can still be activated by heat or oxidative stress independently of the phosphorylation of two conserved Wis1 residues. Evidence is presented that the Pyp1 protein tyrosine phosphatase, which dephosphorylates Spc1, is central to this alternative activation mechanism. The Schizosaccharomyces pombe wis1 super(+) gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of the MAPK homologue Spc1, and integrity of the Wis1-Spc1 pathway is required for survival in extreme conditions of heat, osmolarity, oxidation or limited nutrition. We show here that Wis4, a protein kinase of a new MAPKKK class, phosphorylates Wis1 in vitro and activates it in vivo. Win1 is also required for full activation of Wis1, and Win1 rather than Wis4 mediates the osmotic stress signal. Surprisingly, the pathway can still be activated by heat or oxidative stress independently of the phosphorylation of two conserved Wis1 residues. Evidence is presented that the Pyp1 protein tyrosine phosphatase, which dephosphorylates Spc1, is central to this alternative activation mechanism. |
| Author | Mackie, Shaun Fantes, Peter A. Samejima, Itaru |
| AuthorAffiliation | Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK |
| AuthorAffiliation_xml | – name: Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK |
| Author_xml | – sequence: 1 givenname: Itaru surname: Samejima fullname: Samejima, Itaru organization: Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, EH9 3JR, Edinburgh, UK – sequence: 2 givenname: Shaun surname: Mackie fullname: Mackie, Shaun organization: Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, EH9 3JR, Edinburgh, UK – sequence: 3 givenname: Peter A. surname: Fantes fullname: Fantes, Peter A. email: p.fantes@ed.ac.uk organization: Institute of Cell and Molecular Biology, University of Edinburgh, Mayfield Road, EH9 3JR, Edinburgh, UK |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9321395$$D View this record in MEDLINE/PubMed |
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| Snippet | The Schizosaccharomyces pombe wis1+ gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of the... The Schizosaccharomyces pombe wis1(+) gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of the... The Schizosaccharomyces pombe wis1 super(+) gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of... |
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| SubjectTerms | Amino Acid Sequence Calcium-Calmodulin-Dependent Protein Kinases - genetics Calcium-Calmodulin-Dependent Protein Kinases - metabolism Cell Cycle - genetics cell cycle control Conserved Sequence Enzyme Activation fission yeast Gene Expression Regulation, Fungal Heat-Shock Response MAP Kinase Kinase Kinases MAP kinase signalling pathway Mitogen-Activated Protein Kinase Kinases Mitogen-Activated Protein Kinases Molecular Sequence Data Osmotic Pressure Oxidative Stress Phosphorylation protein tyrosine phosphatase Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Schizosaccharomyces - cytology Schizosaccharomyces - enzymology Schizosaccharomyces - genetics Schizosaccharomyces pombe Proteins Sequence Homology, Amino Acid Signal Transduction stress response |
| Title | Multiple modes of activation of the stress-responsive MAP kinase pathway in fission yeast |
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