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Rck1 and Rck2 MAPKAP kinases and the HOG pathway are required for oxidative stress resistance

Summary We demonstrate a role in oxidative and metal stress resistance for the MAPK‐activated protein kinases Rck1 and Rck2 in Saccharomyces cerevisiae. We show that Hog1 is robustly phosphorylated in a Pbs2‐dependent way during oxidative stress, and that Rck2 also is phosphorylated under these circ...

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Published in:Molecular microbiology 2004-09, Vol.53 (6), p.1743-1756
Main Authors: Bilsland, Elizabeth, Molin, Claes, Swaminathan, Swarna, Ramne, Anna, Sunnerhagen, Per
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cited_by cdi_FETCH-LOGICAL-c6068-4c143b149757e6ef4e56c989ef557984c25fc5a323142a3620fa3bbd05147e8d3
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container_end_page 1756
container_issue 6
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container_title Molecular microbiology
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creator Bilsland, Elizabeth
Molin, Claes
Swaminathan, Swarna
Ramne, Anna
Sunnerhagen, Per
description Summary We demonstrate a role in oxidative and metal stress resistance for the MAPK‐activated protein kinases Rck1 and Rck2 in Saccharomyces cerevisiae. We show that Hog1 is robustly phosphorylated in a Pbs2‐dependent way during oxidative stress, and that Rck2 also is phosphorylated under these circumstances. Hog1 concentrates in the nucleus in oxidative stress. Hog1 localization is partially dependent on Rck2, as rck2 cells have more nuclear Hog1 than wild‐type cells. We find several proteins with a role in oxidative stress resistance using Rck1 or Rck2 as baits in a two‐hybrid screen. We identify the transcription factor Yap2 as a putative target for Rck1, and the Zn2+ transporter Zrc1 as a target for Rck2. Yap2 is normally cytoplasmic, but rapidly migrates to the nucleus upon exposure to oxidative stress agents. In a fraction of untreated pbs2 cells, Yap2 is nuclear. Zrc1 co‐immunoprecipitates with Rck2, and ZRC1 is genetically downstream of RCK2. These data connect activation of the Hog1 MAPK cascade with effectors having a role in oxidative stress resistance.
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We show that Hog1 is robustly phosphorylated in a Pbs2‐dependent way during oxidative stress, and that Rck2 also is phosphorylated under these circumstances. Hog1 concentrates in the nucleus in oxidative stress. Hog1 localization is partially dependent on Rck2, as rck2 cells have more nuclear Hog1 than wild‐type cells. We find several proteins with a role in oxidative stress resistance using Rck1 or Rck2 as baits in a two‐hybrid screen. We identify the transcription factor Yap2 as a putative target for Rck1, and the Zn2+ transporter Zrc1 as a target for Rck2. Yap2 is normally cytoplasmic, but rapidly migrates to the nucleus upon exposure to oxidative stress agents. In a fraction of untreated pbs2 cells, Yap2 is nuclear. Zrc1 co‐immunoprecipitates with Rck2, and ZRC1 is genetically downstream of RCK2. 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Psychology ; Metals - metabolism ; Microbiology ; Mitogen-Activated Protein Kinase Kinases - metabolism ; Mitogen-Activated Protein Kinases - genetics ; Mitogen-Activated Protein Kinases - metabolism ; Oxidative Stress ; Phosphorylation ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Signal Transduction - physiology ; tert-Butylhydroperoxide - metabolism ; Transcription Factors - metabolism ; Two-Hybrid System Techniques</subject><ispartof>Molecular microbiology, 2004-09, Vol.53 (6), p.1743-1756</ispartof><rights>2004 INIST-CNRS</rights><rights>Copyright Blackwell Scientific Publications Ltd. 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We show that Hog1 is robustly phosphorylated in a Pbs2‐dependent way during oxidative stress, and that Rck2 also is phosphorylated under these circumstances. Hog1 concentrates in the nucleus in oxidative stress. Hog1 localization is partially dependent on Rck2, as rck2 cells have more nuclear Hog1 than wild‐type cells. We find several proteins with a role in oxidative stress resistance using Rck1 or Rck2 as baits in a two‐hybrid screen. We identify the transcription factor Yap2 as a putative target for Rck1, and the Zn2+ transporter Zrc1 as a target for Rck2. Yap2 is normally cytoplasmic, but rapidly migrates to the nucleus upon exposure to oxidative stress agents. In a fraction of untreated pbs2 cells, Yap2 is nuclear. Zrc1 co‐immunoprecipitates with Rck2, and ZRC1 is genetically downstream of RCK2. 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subjects Animals
Biological and medical sciences
Cation Transport Proteins - genetics
Cation Transport Proteins - metabolism
Cell Nucleus - metabolism
Fundamental and applied biological sciences. Psychology
Metals - metabolism
Microbiology
Mitogen-Activated Protein Kinase Kinases - metabolism
Mitogen-Activated Protein Kinases - genetics
Mitogen-Activated Protein Kinases - metabolism
Oxidative Stress
Phosphorylation
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Signal Transduction - physiology
tert-Butylhydroperoxide - metabolism
Transcription Factors - metabolism
Two-Hybrid System Techniques
title Rck1 and Rck2 MAPKAP kinases and the HOG pathway are required for oxidative stress resistance
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