naa a22 4500 510745997 CHVBK 20180411083046.0 cr unu---uuuuu 180411e20130501xx s 000 0 eng 10.1007/s12192-012-0382-y doi (NATIONALLICENCE)springer-10.1007/s12192-012-0382-y The p38 MAPK PMK-1 shows heat-induced nuclear translocation, supports chaperone expression, and affects the heat tolerance of Caenorhabditis elegan s [Elektronische Daten] [Ansgar Mertenskötter, Alex Keshet, Peter Gerke, Rüdiger Paul] The p38 mitogen-activated protein kinase PMK-1 of Caenorhabditis elegans has been associated with heavy metal, oxidative and pathogen stress. Pmk-1 is part of an operon comprising three p38 homologues, with pmk-1 expression suggested to be regulated by the operon promoter. There are contradictory reports about the cellular localization of PMK-1. We were interested to study principles of pmk-1 expression and to analyze the role of PMK-1 under heat stress. Using a translational GFP reporter, we found pmk-1 expression to be driven by a promoter in front of pmk-1. PMK-1 was detected in intestinal cells and neurons, with a cytoplasmic localization at moderate temperature. Increasing temperature above 32°C, however, induced a nuclear translocation of PMK-1 as well as PMK-1 accumulation near to apical membranes. Testing survival rates revealed 34-35°C as critical temperature range, where short-term survival severely decreased. Mutants of the PMK-1 pathway (pmk-1Δ, sek-1Δ, mek-1Δ) as well as a mutant of JNK pathway (jnk-1Δ) showed significantly lower survival rates than wild-type or mutants of other pathways (kgb-1Δ, daf-2Δ). Rescue and overexpression experiments verified the negative effects of pmk-1Δ on heat tolerance. Studying gene expression by RNA-seq and semi-quantitative reverse transcriptase polymerase chain reaction revealed positive effects of the PMK-1 pathway on the expression of genes for chaperones, protein biosynthesis, protein degradation, and other functional categories. Thus, the PMK-1 pathway is involved in the heat stress responses of C. elegans, possibly by a PMK-1-mediated activation of the transcription factor SKN-1 and/or an indirect or direct PMK-1-dependent activation (hyperphosphorylation) of heat-shock factor 1. Cell Stress Society International, 2012 DAF-2 nationallicence HSF-1 nationallicence HSP nationallicence SKN-1 nationallicence TOR nationallicence Mertenskötter Ansgar Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut Keshet Alex Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut Gerke Peter Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut Paul Rüdiger Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut Cell Stress and Chaperones Springer Netherlands 18/3(2013-05-01), 293-306 1355-8145 18:3<293 2013 18 12192 https://doi.org/10.1007/s12192-012-0382-y text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s12192-012-0382-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Mertenskötter Ansgar Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut NATIONALLICENCE 700 1- Keshet Alex Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut NATIONALLICENCE 700 1- Gerke Peter Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut NATIONALLICENCE 700 1- Paul Rüdiger Institute of Zoophysiology, University of Münster, Schlossplatz 8, 48143, Münster, Germany aut NATIONALLICENCE 773 0- Cell Stress and Chaperones Springer Netherlands 18/3(2013-05-01), 293-306 1355-8145 18:3<293 2013 18 12192 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer