A phosphatase‐centric mechanism drives stress signaling response
| Autor: | Gabriela Gérecová, Egon Ogris, Natalie Romanov, Jessica Ferrari, Reinhard Beyer, Christoph Schüller, Jiri Veis, Marion Janschitz, David Maria Hollenstein, Wolfgang Reiter, Gustav Ammerer, Markus Hartl |
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| Rok vydání: | 2021 |
| Předmět: |
Proteomics
Cell physiology Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae Phosphatase Cell Cycle Proteins Biochemistry Article phosphatase Post-translational Modifications & Proteolysis Genetics Protein Phosphatase 2 Phosphorylation Molecular Biology hyperosmotic stress signaling biology Effector Chemistry Mechanism (biology) Kinase Articles Protein phosphatase 2 biology.organism_classification greatwall kinase PP2A Cell biology endosulfine Signal Transduction |
| Zdroj: | EMBO Reports |
| ISSN: | 1469-3178 1469-221X |
| Popis: | Changing environmental cues lead to the adjustment of cellular physiology by phosphorylation signaling networks that typically center around kinases as active effectors and phosphatases as antagonistic elements. Here, we report a signaling mechanism that reverses this principle. Using the hyperosmotic stress response in Saccharomyces cerevisiae as a model system, we find that a phosphatase‐driven mechanism causes induction of phosphorylation. The key activating step that triggers this phospho‐proteomic response is the Endosulfine‐mediated inhibition of protein phosphatase 2A‐Cdc55 (PP2ACdc55), while we do not observe concurrent kinase activation. In fact, many of the stress‐induced phosphorylation sites appear to be direct substrates of the phosphatase, rendering PP2ACdc55 the main downstream effector of a signaling response that operates in parallel and independent of the well‐established kinase‐centric stress signaling pathways. This response affects multiple cellular processes and is required for stress survival. Our results demonstrate how a phosphatase can assume the role of active downstream effectors during signaling and allow re‐evaluating the impact of phosphatases on shaping the phosphorylome. The phosphatase PP2ACdc55 assumes the role of an active downstream effector during hyperosmotic stress signaling in Saccharomyces cerevisiae. Inhibition of the phosphatase is the key event resulting in increased phosphorylation, while induction of kinases affecting the same substrates appears not to be required. |
| Databáze: | OpenAIRE |
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