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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 |
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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. |
doi_str_mv | 10.1111/j.1365-2958.2004.04238.x |
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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.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2004.04238.x</identifier><identifier>PMID: 15341652</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>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</subject><ispartof>Molecular microbiology, 2004-09, Vol.53 (6), p.1743-1756</ispartof><rights>2004 INIST-CNRS</rights><rights>Copyright Blackwell Scientific Publications Ltd. Sep 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6068-4c143b149757e6ef4e56c989ef557984c25fc5a323142a3620fa3bbd05147e8d3</citedby><cites>FETCH-LOGICAL-c6068-4c143b149757e6ef4e56c989ef557984c25fc5a323142a3620fa3bbd05147e8d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16112590$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15341652$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bilsland, Elizabeth</creatorcontrib><creatorcontrib>Molin, Claes</creatorcontrib><creatorcontrib>Swaminathan, Swarna</creatorcontrib><creatorcontrib>Ramne, Anna</creatorcontrib><creatorcontrib>Sunnerhagen, Per</creatorcontrib><title>Rck1 and Rck2 MAPKAP kinases and the HOG pathway are required for oxidative stress resistance</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><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.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cation Transport Proteins - genetics</subject><subject>Cation Transport Proteins - metabolism</subject><subject>Cell Nucleus - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Metals - metabolism</subject><subject>Microbiology</subject><subject>Mitogen-Activated Protein Kinase Kinases - metabolism</subject><subject>Mitogen-Activated Protein Kinases - genetics</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Oxidative Stress</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Signal Transduction - physiology</subject><subject>tert-Butylhydroperoxide - metabolism</subject><subject>Transcription Factors - metabolism</subject><subject>Two-Hybrid System Techniques</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNqNkUtr3DAQgEVoSDbb_IUgCu3Nrt6WDz0sIS-aJaG00EsRWnlMtPHaG8ludv995ezSQC6tLho03wyj-RDClOQ0nc_LnHIlM1ZKnTNCRE4E4zrfHKDJ38Q7NCGlJBnX7OcxOolxSQjlRPEjdEwlF1RJNkG_vrlHim1b4RQwPJ_df53d40ff2gjx5b1_AHx9d4XXtn94tltsA-AAT4MPUOG6C7jb-Mr2_jfg2AeIMWWjj71tHbxHh7VtIpzu7yn6cXnx_fw6u727ujmf3WZOEaUz4ajgCyrKQhagoBYglSt1CbWURamFY7J20nLGqWCWK0ZqyxeLikgqCtAVn6JPu77r0D0NEHuz8tFB09gWuiEapbSgulD_BKkmaaK0pyn68AZcdkNo0ycMLZUcubGb3kEudDEGqM06-JUNW0OJGUWZpRl9mNGHGUWZF1Fmk0rP9v2HxQqq18K9mQR83AM2OtvUIe3Tx1dOUcpkSRL3Zcc9-wa2_z2Amc9vxoj_AeW9q4c</recordid><startdate>200409</startdate><enddate>200409</enddate><creator>Bilsland, Elizabeth</creator><creator>Molin, Claes</creator><creator>Swaminathan, Swarna</creator><creator>Ramne, Anna</creator><creator>Sunnerhagen, Per</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</general><general>Blackwell Publishing Ltd</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200409</creationdate><title>Rck1 and Rck2 MAPKAP kinases and the HOG pathway are required for oxidative stress resistance</title><author>Bilsland, Elizabeth ; Molin, Claes ; Swaminathan, Swarna ; Ramne, Anna ; Sunnerhagen, Per</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6068-4c143b149757e6ef4e56c989ef557984c25fc5a323142a3620fa3bbd05147e8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cation Transport Proteins - genetics</topic><topic>Cation Transport Proteins - metabolism</topic><topic>Cell Nucleus - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Metals - metabolism</topic><topic>Microbiology</topic><topic>Mitogen-Activated Protein Kinase Kinases - metabolism</topic><topic>Mitogen-Activated Protein Kinases - genetics</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Oxidative Stress</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Signal Transduction - physiology</topic><topic>tert-Butylhydroperoxide - metabolism</topic><topic>Transcription Factors - metabolism</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bilsland, Elizabeth</creatorcontrib><creatorcontrib>Molin, Claes</creatorcontrib><creatorcontrib>Swaminathan, Swarna</creatorcontrib><creatorcontrib>Ramne, Anna</creatorcontrib><creatorcontrib>Sunnerhagen, Per</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bilsland, Elizabeth</au><au>Molin, Claes</au><au>Swaminathan, Swarna</au><au>Ramne, Anna</au><au>Sunnerhagen, Per</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rck1 and Rck2 MAPKAP kinases and the HOG pathway are required for oxidative stress resistance</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2004-09</date><risdate>2004</risdate><volume>53</volume><issue>6</issue><spage>1743</spage><epage>1756</epage><pages>1743-1756</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>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.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15341652</pmid><doi>10.1111/j.1365-2958.2004.04238.x</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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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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