Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG map kinase pathway
| Autor: | M. C. Kelders, Willem H. Mager, Marco Siderius, Vladimír Reiser, O.C.M.C. van Wuytswinkel, Helmut Ruis, Gustav Ammerer |
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| Přispěvatelé: | Biochemistry and Molecular Biology, Chemistry and Pharmaceutical Sciences, Molecular and Computational Toxicology |
| Jazyk: | angličtina |
| Rok vydání: | 2000 |
| Předmět: |
MAPK/ERK pathway
Saccharomyces cerevisiae Proteins Osmotic shock p38 mitogen-activated protein kinases Saccharomyces cerevisiae Blotting Western Protein Tyrosine Phosphatase Non-Receptor Type 11 macromolecular substances Protein tyrosine phosphatase Microbiology Osmotic Pressure Phosphorylation Molecular Biology biology Protein Tyrosine Phosphatase Non-Receptor Type 6 Intracellular Signaling Peptides and Proteins biology.organism_classification Cell biology Biochemistry Microscopy Fluorescence Mitogen-activated protein kinase biology.protein Signal transduction Mitogen-Activated Protein Kinases Protein Tyrosine Phosphatases Signal Transduction |
| Zdroj: | Molecular Microbiology, 37(2), 382-397. Wiley-Blackwell van Wuytswinkel, O, Reiser, V, Siderius, M H, Kelders, M, Ammerer, G, Ruis, H & Mager, W H 2000, ' Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG map kinase pathway ', Molecular Microbiology, vol. 37, no. 2, pp. 382-397 . https://doi.org/10.1046/j.1365-2958.2000.02002.x |
| ISSN: | 0950-382X |
| Popis: | The HOG/p38 MAP kinase route is an important stress-activated signal transduction pathway that is well conserved among eukaryotes. Here, we describe a novel mechanism of activation of the HOG pathway in budding yeast. This mechanism operates upon severe osmostress conditions (1.4 M NaCl) and is independent of the Sln1p and Sho1p osmosensors. The alternative input feeds into the HOG pathway MAPKK Pbs2p and requires activation of Pbs2p by phosphorylation. We show that, upon severe osmotic shock, Hog1p nuclear accumulation and phosphorylation is delayed compared with mild stress. Moreover, both events lost their transient pattern, presumably because of the absence of negative feedback mediated by Ptp2p tyrosine phosphatase, which we found to be localized in the nucleus. Under severe osmotic stress conditions, the delayed nuclear accumulation correlates with a delay in stress-responsive gene expression. Severe osmoshock leads to a situation in which active and nuclear-localized Hog1p is transiently unable to induce transcription of osmotic stress-responsive genes. It also appeared from our studies that the Sho1p osmosensor is less active under severe osmotic stress conditions, whereas the Sln1p/Ypd1p/Ssk1p sensor and signal transducer functions normally under these circumstances. |
| Databáze: | OpenAIRE |
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