PP2A Rts1 antagonizes Rck2-mediated hyperosmotic stress signaling in yeast.

Autor: Hollenstein DM; Department of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria., Veis J; Department of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria; Center for Medical Biochemistry, Max Perutz Labs, Medical University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria., Romanov N; Max Planck Institute of Biophysics, Max-von-Laue Straße 3, 60438 Frankfurt am Main, Germany., Gérecová G; Department of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria., Ogris E; Center for Medical Biochemistry, Max Perutz Labs, Medical University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria., Hartl M; Mass Spectrometry Facility, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria., Ammerer G; Department of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria., Reiter W; Department of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria; Mass Spectrometry Facility, Max Perutz Labs, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9, 1030 Vienna, Austria. Electronic address: wolfgang.l.reiter@univie.ac.at.
Jazyk: angličtina
Zdroj: Microbiological research [Microbiol Res] 2022 Jul; Vol. 260, pp. 127031. Date of Electronic Publication: 2022 Apr 11.
DOI: 10.1016/j.micres.2022.127031
Abstrakt: 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.
(Copyright © 2022 The Authors. Published by Elsevier GmbH.. All rights reserved.)
Databáze: MEDLINE
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