Evidence map›Paper›PMID 34558777›Full record

ArticleEMBO reports2021

A phosphatase-centric mechanism drives stress signaling response.

David Maria Hollenstein, Gabriela Gérecová, Natalie Romanov, Jessica Ferrari, Jiri Veis, Marion Janschitz, Reinhard Beyer, Christoph Schüller, Egon Ogris, Markus Hartl and 2 more

Abstract read
In one paragraph

Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. An AI-Ready Phosphorylation Meta-Analysis forJournal of proteome research · 2026
    Pooled it
  2. Article
  3. Article
  4. Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024
    Article
  5. Review
  6. Article
  7. Review
  8. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

David Maria HollensteinDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0002-1977-1556
Gabriela GérecováDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0003-2014-0556
Natalie RomanovMax Planck Institute of Biophysics, Frankfurt am Main, Germany.ORCID 0000-0003-3749-2654
Jessica FerrariDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.
Jiri VeisDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0002-4215-3115
Marion JanschitzDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0003-1151-0228
Reinhard BeyerDepartment of Applied Genetics and Cell Biology (DAGZ), University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.ORCID 0000-0002-0516-6742
Christoph SchüllerDepartment of Applied Genetics and Cell Biology (DAGZ), University of Natural Resources and Life Sciences (BOKU), Vienna, Austria.ORCID 0000-0002-1649-1217
Egon OgrisCenter for Medical Biochemistry, Max Perutz Labs, Vienna BioCenter, Medical University of Vienna, Vienna, Austria.ORCID 0000-0001-5950-9264
Markus HartlDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0002-4970-7336
Gustav AmmererDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.
Wolfgang ReiterDepartment of Biochemistry and Cell Biology, Max Perutz Labs, Vienna BioCenter (VBC), University of Vienna, Vienna, Austria.ORCID 0000-0003-1266-8975

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 (PP2A

Indexed as

Saccharomyces cerevisiae ProteinsCell Cycle ProteinsPhosphorylationProtein Phosphatase 2ProteomicsSaccharomyces cerevisiaeCDC55 protein, S cerevisiaeCell Cycle ProteinsProtein Phosphatase 2Saccharomyces cerevisiae Proteinsendosulfinegreatwall kinasehyperosmotic stress signalingphosphatasePP2A

Identifiers

PMID34558777
PMCPMC8567219

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.