PP2ARts1 antagonizes Rck2-mediated hyperosmotic stress signaling in yeast
In Saccharomyces cerevisiae, impairment of protein phosphatase PP2ARts1 leads to temperature and hyperosmotic stress sensitivity, yet the underlying mechanism and the scope of action of the phosphatase in the stress response remain elusive. Using a quantitative mass spectrometry-based approach we ha...
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| Veröffentlicht in: | Microbiological research 2022-07, Vol.260, p.127031-127031, Article 127031 |
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| container_title | Microbiological research |
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| creator | Hollenstein, D.M. Veis, J. Romanov, N. Gérecová, G. Ogris, E. Hartl, M. Ammerer, G. Reiter, W. |
| description | In Saccharomyces cerevisiae, impairment of protein phosphatase PP2ARts1 leads to temperature and hyperosmotic stress sensitivity, yet the underlying mechanism and the scope of action of the phosphatase in the stress response remain elusive. Using a quantitative mass spectrometry-based approach we have identified a set of putative substrate proteins that show both hyperosmotic stress- and PP2ARts1-dependent changes in their phosphorylation pattern. A comparative analysis with published MS-shotgun data revealed that the phosphorylation status of many of these sites is regulated by the MAPKAP kinase Rck2, suggesting that the phosphatase antagonizes Rck2 signaling. Detailed gel mobility shift assays and protein-protein interaction analysis strongly indicate that Rck2 activity is directly regulated by PP2ARts1 via a SLiM B56-family interaction motif, revealing how PP2ARts1 influences the response to hyperosmotic stress in Yeast. |
| doi_str_mv | 10.1016/j.micres.2022.127031 |
| format | Article |
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Using a quantitative mass spectrometry-based approach we have identified a set of putative substrate proteins that show both hyperosmotic stress- and PP2ARts1-dependent changes in their phosphorylation pattern. A comparative analysis with published MS-shotgun data revealed that the phosphorylation status of many of these sites is regulated by the MAPKAP kinase Rck2, suggesting that the phosphatase antagonizes Rck2 signaling. 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Using a quantitative mass spectrometry-based approach we have identified a set of putative substrate proteins that show both hyperosmotic stress- and PP2ARts1-dependent changes in their phosphorylation pattern. A comparative analysis with published MS-shotgun data revealed that the phosphorylation status of many of these sites is regulated by the MAPKAP kinase Rck2, suggesting that the phosphatase antagonizes Rck2 signaling. Detailed gel mobility shift assays and protein-protein interaction analysis strongly indicate that Rck2 activity is directly regulated by PP2ARts1 via a SLiM B56-family interaction motif, revealing how PP2ARts1 influences the response to hyperosmotic stress in Yeast.</description><subject>gels</subject><subject>Hog1</subject><subject>Hyperosmotic stress</subject><subject>mass spectrometry</subject><subject>Phosphatase</subject><subject>Phosphorylation</subject><subject>PP2A</subject><subject>protein-protein interactions</subject><subject>Quantitative proteomics</subject><subject>Rck2</subject><subject>Rts1</subject><subject>Saccharomyces cerevisiae</subject><subject>Stress response</subject><subject>Stress signaling</subject><subject>temperature</subject><subject>yeasts</subject><issn>0944-5013</issn><issn>1618-0623</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNqNkEtPwzAQhC0EEqXwDzjkyCVh13YeviBVFY9KlagqOFuusykueRQ7IJVfT6pwRlx2LjOzmo-xa4QEAbPbXdI46ykkHDhPkOcg8IRNMMMihoyLUzYBJWWcAopzdhHCDgClKviELVYrPlv3ASPT9mbbte6bQrS27zxuqHSmpzJ6O-zJd6Hpemej0A-PQhTctjW1a7eRa6MDmdBfsrPK1IGufnXKXh_uX-ZP8fL5cTGfLWPLkWNscgGVsbQpS0BOmTBqgwpzJAtGQmGAKi7SUpVK5EWay4yGy2W1kdIKi2LKbsbeve8-Pin0unHBUl2blrrPoHmWIYAqRP4Payp5rpQ6tsrRaoelwVOl9941xh80gj5C1js9QtZHyHqEPMTuxhgNi78ceR2so9YO6DzZXped-7vgB8Oyhgs</recordid><startdate>202207</startdate><enddate>202207</enddate><creator>Hollenstein, D.M.</creator><creator>Veis, J.</creator><creator>Romanov, N.</creator><creator>Gérecová, G.</creator><creator>Ogris, E.</creator><creator>Hartl, M.</creator><creator>Ammerer, G.</creator><creator>Reiter, W.</creator><general>Elsevier GmbH</general><scope>6I.</scope><scope>AAFTH</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope></search><sort><creationdate>202207</creationdate><title>PP2ARts1 antagonizes Rck2-mediated hyperosmotic stress signaling in yeast</title><author>Hollenstein, D.M. ; Veis, J. ; Romanov, N. ; Gérecová, G. ; Ogris, E. ; Hartl, M. ; Ammerer, G. ; Reiter, W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2121-a730facebdd012e63a9b19171ec0a408a0ef235d9d93785746e85724fb44c3c13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>gels</topic><topic>Hog1</topic><topic>Hyperosmotic stress</topic><topic>mass spectrometry</topic><topic>Phosphatase</topic><topic>Phosphorylation</topic><topic>PP2A</topic><topic>protein-protein interactions</topic><topic>Quantitative proteomics</topic><topic>Rck2</topic><topic>Rts1</topic><topic>Saccharomyces cerevisiae</topic><topic>Stress response</topic><topic>Stress signaling</topic><topic>temperature</topic><topic>yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hollenstein, D.M.</creatorcontrib><creatorcontrib>Veis, J.</creatorcontrib><creatorcontrib>Romanov, N.</creatorcontrib><creatorcontrib>Gérecová, G.</creatorcontrib><creatorcontrib>Ogris, E.</creatorcontrib><creatorcontrib>Hartl, M.</creatorcontrib><creatorcontrib>Ammerer, G.</creatorcontrib><creatorcontrib>Reiter, W.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Microbiological research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hollenstein, D.M.</au><au>Veis, J.</au><au>Romanov, N.</au><au>Gérecová, G.</au><au>Ogris, E.</au><au>Hartl, M.</au><au>Ammerer, G.</au><au>Reiter, W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PP2ARts1 antagonizes Rck2-mediated hyperosmotic stress signaling in yeast</atitle><jtitle>Microbiological research</jtitle><date>2022-07</date><risdate>2022</risdate><volume>260</volume><spage>127031</spage><epage>127031</epage><pages>127031-127031</pages><artnum>127031</artnum><issn>0944-5013</issn><eissn>1618-0623</eissn><abstract>In Saccharomyces cerevisiae, impairment of protein phosphatase PP2ARts1 leads to temperature and hyperosmotic stress sensitivity, yet the underlying mechanism and the scope of action of the phosphatase in the stress response remain elusive. Using a quantitative mass spectrometry-based approach we have identified a set of putative substrate proteins that show both hyperosmotic stress- and PP2ARts1-dependent changes in their phosphorylation pattern. A comparative analysis with published MS-shotgun data revealed that the phosphorylation status of many of these sites is regulated by the MAPKAP kinase Rck2, suggesting that the phosphatase antagonizes Rck2 signaling. Detailed gel mobility shift assays and protein-protein interaction analysis strongly indicate that Rck2 activity is directly regulated by PP2ARts1 via a SLiM B56-family interaction motif, revealing how PP2ARts1 influences the response to hyperosmotic stress in Yeast.</abstract><pub>Elsevier GmbH</pub><doi>10.1016/j.micres.2022.127031</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| source | Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | gels Hog1 Hyperosmotic stress mass spectrometry Phosphatase Phosphorylation PP2A protein-protein interactions Quantitative proteomics Rck2 Rts1 Saccharomyces cerevisiae Stress response Stress signaling temperature yeasts |
| title | PP2ARts1 antagonizes Rck2-mediated hyperosmotic stress signaling in yeast |
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