Cmk2 kinase is essential for survival in arsenite by modulating translation together with RACK1 orthologue Cpc2 in Schizosaccharomyces pombe
| Autor: | José Cansado, Maria Jesús Pujol, Oriol Bachs, Rosa Aligué, Julia Llanes, Marta Sanchez-Marinas, David Giménez-Zaragoza, Edgar Martin-Ramos |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
MAPK/ERK pathway Arsenites Protein Serine-Threonine Kinases Receptors for Activated C Kinase Biochemistry Ribosome 03 medical and health sciences chemistry.chemical_compound Stress Physiological Physiology (medical) Gene Expression Regulation Fungal Schizosaccharomyces DNA Fungal Transcription factor Arsenite Ribosome Subunits Small Eukaryotic Microbial Viability biology Kinase Translation (biology) biology.organism_classification Cell biology 030104 developmental biology chemistry Protein Biosynthesis Schizosaccharomyces pombe Schizosaccharomyces pombe Proteins Mitogen-Activated Protein Kinases Eukaryotic Ribosome Reactive Oxygen Species Signal Transduction |
| Zdroj: | Free radical biologymedicine. 129 |
| ISSN: | 1873-4596 |
| Popis: | Different studies have demonstrated multiple effects of arsenite on human physiology. However, there are many open questions concerning the mechanism of response to arsenite. Schizosaccharomyces pombe activates the Sty1 MAPK pathway as a common response to several stress conditions. The specificity of the response is due to the activation of different transcription factors and specific targets such the Cmk2 MAPKAP kinase. We have previously shown that Cmk2 is phosphorylated and activated by the MAPK Sty1 in response to oxidative stress. Here, we report that Cmk2 kinase is specifically necessary to overcome the stress caused by metalloid agents, in particular arsenite. Deletion of cmk2 increases the protein level of various components of the MAPK pathway. Moreover, Cmk2 negatively regulates translation through the Cpc2 kinase: the RACK1 orthologue in fission yeast. RACK1 is a receptor for activated C-kinase. Interestingly, RACK1 is a constituent of the eukaryotic ribosome specifically localized in the head region of the 40 S subunit. Cmk2 controls arsenite response through Cpc2 and it does so through Cpc2 ribosomal function, as observed in genetic analysis using a Cpc2 mutant unable to bind to ribosome. These findings suggest a role for Cmk2 in regulating translation and facilitating adaptation to arsenite stress in the ribosome. |
| Databáze: | OpenAIRE |
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