首页|PP2A(Rts1) antagonizes Rck2-mediated hyperosmotic stress signaling in yeast

PP2A(Rts1) antagonizes Rck2-mediated hyperosmotic stress signaling in yeast

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  • NSTL
  • Elsevier
In Saccharomyces cerevisiae, impairment of protein phosphatase PP2A(Rts1) 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 PP2A(Rts1)-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 PP2A(Rts1) via a SLiM B56-family interaction motif, revealing how PP2A(Rts1) influences the response to hyperosmotic stress in Yeast.

PP2ARts1Rck2Stress responsePhosphorylationQuantitative proteomicsPhosphataseHog1Hyperosmotic stressStress signalingSaccharomyces cerevisiaeACTIVATED PROTEIN-KINASEREGULATORY SUBUNITRESPONSE PATHWAYPHOSPHATASE 2ACELL-CULTUREAMINO-ACIDSLOCALIZATIONEXPRESSIONPTP2RCK2

Hollenstein, D. M.、Veis, J.、Romanov, N.、Gerecova, G.、Ogris, E.、Hartl, M.、Ammerer, G.、Reiter, W.

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Univ Vienna

Max Planck Inst Biophys

Med Univ Vienna

2022

10.1016/j.micres.2022.127031

Microbiological Research

Microbiological Research

EISCI
ISSN：0944-5013
年,卷(期)：2022.260
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