Evidence map›Paper›PMID 28940407›Full record

ArticleFEBS letters2017

Redox state-dependent modulation of plant SnRK1 kinase activity differs from AMPK regulation in animals.

Bernhard Wurzinger, Andrea Mair, Katrin Fischer-Schrader, Ella Nukarinen, Valentin Roustan, Wolfram Weckwerth, Markus Teige

Open access · hybridAbstract readLetter
In one paragraph

Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Perception and processing of stress signals by plant mitochondria.The Plant journal : for cell and molecular biology · 2024
    Review
  5. Article
  6. Review
  7. Article
  8. Metabolic regulation of quiescence in plants.The Plant journal : for cell and molecular biology · 2023
    Article
  9. Review
  10. Review
  11. Review
  12. Low nitrogen conditions accelerate flowering by modulating the phosphorylation state of FLOWERING BHLH 4 inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Low UV-C stress modulatesBiotechnology for biofuels · 2020
    Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. 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

7 authors at 3 institutions in 3 countries.

Bernhard WurzingerDepartment of Ecogenomics and Systems Biology, University of Vienna, Austria.
Andrea MairDepartment of Ecogenomics and Systems Biology, University of Vienna, Austria.
Katrin Fischer-SchraderDepartment of Chemistry, Faculty of Mathematics and Natural Sciences, University of Cologne, Germany.
Ella NukarinenDepartment of Ecogenomics and Systems Biology, University of Vienna, Austria.
Valentin RoustanDepartment of Ecogenomics and Systems Biology, University of Vienna, Austria.
Wolfram WeckwerthDepartment of Ecogenomics and Systems Biology, University of Vienna, Austria.
Markus TeigeDepartment of Ecogenomics and Systems Biology, University of Vienna, Austria.
University of Vienna · ATEcogenomics (Japan) · JPUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolutionarily highly conserved SNF1-related protein kinase (SnRK1) protein kinase is a metabolic master regulator in plants, balancing the critical energy consumption between growth- and stress response-related metabolic pathways. While the regulation of the mammalian [AMP-activated protein kinase (AMPK)] and yeast (SNF1) orthologues of SnRK1 is well-characterised, the regulation of SnRK1 kinase activity in plants is still an open question. Here we report that the activity and T-loop phosphorylation of AKIN10, the kinase subunit of the SnRK1 complex, is regulated by the redox status. Although this regulation is dependent on a conserved cysteine residue, the underlying mechanism is different to the redox regulation of animal AMPK and has functional implications for the regulation of the kinase complex in plants under stress conditions.

Indexed as

AMP-Activated Protein KinasesAnimalsArabidopsisArabidopsis ProteinsOxidation-ReductionPhosphorylationProtein Serine-Threonine KinasesStress, PhysiologicalAMP-Activated Protein KinasesArabidopsis ProteinsAt3g01090 protein, ArabidopsisProtein Serine-Threonine KinasesAKIN10protein kinasereactive oxygen speciesredox regulationSnRK1

Identifiers

PMID28940407
PMCPMC5698759
OpenAlexW2759463723

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.