Evidence map›Paper›PMID 27545962›Full record

ArticleScientific reports2016

Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog SnRK1 as a metabolic master regulator under energy deprivation.

Ella Nukarinen, Thomas Nägele, Lorenzo Pedrotti, Bernhard Wurzinger, Andrea Mair, Ramona Landgraf, Frederik Börnke, Johannes Hanson, Markus Teige, Elena Baena-Gonzalez and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 162 papers.

0numbers the graph read from it
0cells of the map it votes in
162citing papers in PubMed
64.4field-weighted citation impact, top 1% 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

162 citing papers in PubMed, 322 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

102 more citing papers are in PubMed but not listed here.

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 at 6 institutions in 4 countries.

Ella NukarinenDepartment of Ecogenomics and Systems Biology, University of Vienna, Vienna, Austria.
Thomas NägeleDepartment of Ecogenomics and Systems Biology, University of Vienna, Vienna, Austria.
Lorenzo PedrottiJulius-von-Sachs-Institut, Julius-Maximilians-Universität Würzburg, Würzburg, Germany.
Bernhard WurzingerDepartment of Ecogenomics and Systems Biology, University of Vienna, Vienna, Austria.
Andrea MairDepartment of Ecogenomics and Systems Biology, University of Vienna, Vienna, Austria.
Ramona LandgrafPlant Health, Plant Metabolism Group, Leibniz-Institute of Vegetable and Ornamental Crops, Großbeeren, Germany.
Frederik BörnkePlant Health, Plant Metabolism Group, Leibniz-Institute of Vegetable and Ornamental Crops, Großbeeren, Germany.
Johannes HansonDepartment of Plant Physiology, Umeå University, Umeå, Sweden.
Markus TeigeDepartment of Ecogenomics and Systems Biology, University of Vienna, Vienna, Austria.
Elena Baena-GonzalezInstituto Gulbenkian de Ciência, Oeiras, Portugal.
Wolfgang Dröge-LaserJulius-von-Sachs-Institut, Julius-Maximilians-Universität Würzburg, Würzburg, Germany.
Wolfram WeckwerthDepartment of Ecogenomics and Systems Biology, University of Vienna, Vienna, Austria.
University of Vienna · ATUniversity of Würzburg · DEInstituto Gulbenkian de Ciência · PTLeibniz Institute of Vegetable and Ornamental Crops · DEUmeå University · SEUniversity of Potsdam · DE

Funding

Austrian Science Fund FWF P 25488
6 · The paper itself

Abstract

Since years, research on SnRK1, the major cellular energy sensor in plants, has tried to define its role in energy signalling. However, these attempts were notoriously hampered by the lethality of a complete knockout of SnRK1. Therefore, we generated an inducible amiRNA::SnRK1α2 in a snrk1α1 knock out background (snrk1α1/α2) to abolish SnRK1 activity to understand major systemic functions of SnRK1 signalling under energy deprivation triggered by extended night treatment. We analysed the in vivo phosphoproteome, proteome and metabolome and found that activation of SnRK1 is essential for repression of high energy demanding cell processes such as protein synthesis. The most abundant effect was the constitutively high phosphorylation of ribosomal protein S6 (RPS6) in the snrk1α1/α2 mutant. RPS6 is a major target of TOR signalling and its phosphorylation correlates with translation. Further evidence for an antagonistic SnRK1 and TOR crosstalk comparable to the animal system was demonstrated by the in vivo interaction of SnRK1α1 and RAPTOR1B in the cytosol and by phosphorylation of RAPTOR1B by SnRK1α1 in kinase assays. Moreover, changed levels of phosphorylation states of several chloroplastic proteins in the snrk1α1/α2 mutant indicated an unexpected link to regulation of photosynthesis, the main energy source in plants.

Indexed as

ProteomicsArabidopsisArabidopsis ProteinsEnergy MetabolismPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesArabidopsis ProteinsAt3g01090 protein, ArabidopsisPhosphoproteinsProtein Serine-Threonine Kinases

Identifiers

PMID27545962
PMCPMC4992866
OpenAlexW2511143602

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.