Identifying protein kinase–specific effectors of the osmostress response in yeast
| Autor: | David Maria Hollenstein, Gustav Ammerer, Natalie Romanov, Marion Janschitz, Dorothea Anrather, Wolfgang Reiter |
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| Rok vydání: | 2017 |
| Předmět: |
Proteomics
0301 basic medicine MAPK/ERK pathway Saccharomyces cerevisiae Proteins Proteome p38 mitogen-activated protein kinases Saccharomyces cerevisiae Protein Serine-Threonine Kinases Biochemistry Mass Spectrometry Article 03 medical and health sciences 0302 clinical medicine Osmotic Pressure Phosphorylation Protein kinase A Molecular Biology biology Effector Kinase Osmolar Concentration Cell Biology Phosphoproteins biology.organism_classification 030104 developmental biology Mutation Mitogen-Activated Protein Kinases Signal transduction 030217 neurology & neurosurgery Signal Transduction |
| Zdroj: | Science Signaling. 10 |
| ISSN: | 1937-9145 1945-0877 |
| Popis: | The budding yeast Saccharomyces cerevisiae reacts to increased external osmolarity by modifying many cellular processes. Adaptive signaling relies primarily on the high-osmolarity glycerol (HOG) pathway, which is closely related to the mammalian p38 mitogen-activated protein kinase (MAPK) pathway in core architecture. To identify target proteins of the MAPK Hog1, we designed a mass spectrometry-based high-throughput experiment to measure the impact of Hog1 activation or inhibition on the Scerevisiae phosphoproteome. In addition, we analyzed how deletion of RCK2, which encodes a known effector protein kinase target of Hog1, modulated osmotic stress-induced phosphorylation. Our results not only provide an overview of the diversity of cellular functions that are directly and indirectly affected by the activity of the HOG pathway but also enabled an assessment of the Hog1-independent events that occur under osmotic stress conditions. We extended the number of putative Hog1 direct targets by analyzing the modulation of motifs consisting of serine or threonine followed by a proline (S/T-P motif) and subsequently validated these with an in vivo interaction assay. Rck2 appears to act as a central hub for many Hog1-mediated secondary phosphorylation events. This study clarifies many of the direct and indirect effects of HOG signaling and its stress-adaptive functions. |
| Databáze: | OpenAIRE |
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