Evidence map›Paper›PMID 35818121›Full record

ArticleThe Plant cell2022

Endoplasmic reticulum oxidoreductin provides resilience against reductive stress and hypoxic conditions by mediating luminal redox dynamics.

José Manuel Ugalde, Isabel Aller, Lika Kudrjasova, Romy R Schmidt, Michelle Schlößer, Maria Homagk, Philippe Fuchs, Sophie Lichtenauer, Markus Schwarzländer, Stefanie J Müller-Schüssele and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
8.4field-weighted citation impact, top 2% of its field
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

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. A family of NADPH/NADPNature communications · 2024
    Article
  10. Review
  11. Review
  12. Review
  13. Visualizing Orientation and Topology of ER Membrane Proteins In Planta.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  14. Lighting the light reactions of photosynthesis by means of redox-responsive genetically encoded biosensors for photosynthetic intermediates.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. The Passage of HPlants (Basel, Switzerland) · 2022
    Review
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

11 authors at 3 institutions in 1 country.

José Manuel UgaldeINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.ORCID 0000-0002-0601-4302
Isabel AllerINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.
Lika KudrjasovaINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.ORCID 0000-0003-1205-5845
Romy R SchmidtPlant Biotechnology, Bielefeld University, D-33615 Bielefeld, Germany.ORCID 0000-0002-3395-0673
Michelle SchlößerINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.ORCID 0000-0001-6913-8356
Maria HomagkINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.ORCID 0000-0002-8952-848X
Philippe FuchsINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.ORCID 0000-0001-6379-853X
Sophie LichtenauerInstitute for Biology and Biotechnology of Plants, University of Münster, D-48143 Münster, Germany.ORCID 0000-0003-4525-6555
Markus SchwarzländerInstitute for Biology and Biotechnology of Plants, University of Münster, D-48143 Münster, Germany.ORCID 0000-0003-0796-8308
Stefanie J Müller-SchüsseleINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.ORCID 0000-0003-4061-1175
Andreas J MeyerINRES-Chemical Signalling, University of Bonn, D-53113 Bonn, Germany.ORCID 0000-0001-8144-4364
University of Bonn · DEUniversity of Münster · DEBielefeld University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidative protein folding in the endoplasmic reticulum (ER) depends on the coordinated action of protein disulfide isomerases and ER oxidoreductins (EROs). Strict dependence of ERO activity on molecular oxygen as the final electron acceptor implies that oxidative protein folding and other ER processes are severely compromised under hypoxia. Here, we isolated viable Arabidopsis thaliana ero1 ero2 double mutants that are highly sensitive to reductive stress and hypoxia. To elucidate the specific redox dynamics in the ER in vivo, we expressed the glutathione redox potential (EGSH) sensor Grx1-roGFP2iL-HDEL with a midpoint potential of -240 mV in the ER of Arabidopsis plants. We found EGSH values of -241 mV in wild-type plants, which is less oxidizing than previously estimated. In the ero1 ero2 mutants, luminal EGSH was reduced further to -253 mV. Recovery to reductive ER stress induced by dithiothreitol was delayed in ero1 ero2. The characteristic signature of EGSH dynamics in the ER lumen triggered by hypoxia was affected in ero1 ero2 reflecting a disrupted balance of reductive and oxidizing inputs, including nascent polypeptides and glutathione entry. The ER redox dynamics can now be dissected in vivo, revealing a central role of EROs as major redox integrators to promote luminal redox homeostasis.

Indexed as

ArabidopsisProtein Disulfide-IsomerasesDithiothreitolEndoplasmic ReticulumEndoplasmic Reticulum StressGlutathioneHypoxiaOxidation-ReductionOxygenProtein FoldingDithiothreitolGlutathioneOxygenProtein Disulfide-Isomerases

Identifiers

PMID35818121
PMCPMC9516139
OpenAlexW4285041675

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.