PP2ARts1 antagonizes Rck2-mediated hyperosmotic stress signaling in yeast.

D M Hollenstein, J Veis, N Romanov, G Gérecová, E Ogris, M Hartl, G Ammerer, W Reiter

Microbiological research 2022 Jul

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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. Copyright © 2022 The Authors. Published by Elsevier GmbH.. All rights reserved.

Citation

D M Hollenstein, J Veis, N Romanov, G Gérecová, E Ogris, M Hartl, G Ammerer, W Reiter. PP2ARts1 antagonizes Rck2-mediated hyperosmotic stress signaling in yeast. Microbiological research. 2022 Jul;260:127031