Evidence map›Paper›PMID 32908151›Full record

ArticleNature communications2020

A moonlighting role for enzymes of glycolysis in the co-localization of mitochondria and chloroplasts.

Youjun Zhang, Arun Sampathkumar, Sandra Mae-Lin Kerber, Corné Swart, Carsten Hille, Kumar Seerangan, Alexander Graf, Lee Sweetlove, Alisdair R Fernie

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Hyperspectral phenotyping and GWAS identify novel QTLs for soybean photosynthetic rate.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
    Article
  3. Review
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  5. TheProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Loss ofPlants (Basel, Switzerland) · 2026
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  10. Proviral insights of glycolytic enolase inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Review
  13. Review
  14. Article
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  16. Review
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  19. Plastid Transient and Stable Interactions with Other Cell Compartments.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  20. 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

9 authors at 4 institutions in 3 countries.

Youjun ZhangMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany. Yozhang@mpimp-golm.mpg.de.ORCID http://orcid.org/0000-0003-1052-0256
Arun SampathkumarMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany.ORCID http://orcid.org/0000-0003-1703-0137
Sandra Mae-Lin KerberMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany.ORCID http://orcid.org/0000-0001-7929-8919
Corné SwartMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany.
Carsten HilleDepartment of Physical Chemistry, University of Potsdam, Karl-Liebknecht-Strasse 24-25, 14476, Potsdam-Golm, Germany.ORCID http://orcid.org/0000-0003-3454-8077
Kumar SeeranganMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany.
Alexander GrafMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany.
Lee SweetloveDepartment of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK.ORCID http://orcid.org/0000-0002-2461-4133
Alisdair R FernieMax-Planck-Institut für Molekulare Pflanzenphysiologie, Am Mühlenberg 1, 14476, Potsdam-Golm, Germany. fernie@mpimp-golm.mpg.de.ORCID http://orcid.org/0000-0001-9000-335X
Max Planck Institute of Molecular Plant Physiology · DECenter of Plant Systems Biology and Biotechnology · BGUniversity of Oxford · GBUniversity of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycolysis is one of the primordial pathways of metabolism, playing a pivotal role in energy metabolism and biosynthesis. Glycolytic enzymes are known to form transient multi-enzyme assemblies. Here we examine the wider protein-protein interactions of plant glycolytic enzymes and reveal a moonlighting role for specific glycolytic enzymes in mediating the co-localization of mitochondria and chloroplasts. Knockout mutation of phosphoglycerate mutase or enolase resulted in a significantly reduced association of the two organelles. We provide evidence that phosphoglycerate mutase and enolase form a substrate-channelling metabolon which is part of a larger complex of proteins including pyruvate kinase. These results alongside a range of genetic complementation experiments are discussed in the context of our current understanding of chloroplast-mitochondrial interactions within photosynthetic eukaryotes.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsEnergy MetabolismGlycolysisMitochondriaMutationPhosphoglycerate MutasePhosphopyruvate HydratasePhotosynthesisPlants, Genetically ModifiedProtein Interaction MappingProtein Interaction MapsPyruvate KinaseArabidopsis ProteinsPhosphoglycerate MutasePhosphopyruvate HydratasePyruvate Kinase

Identifiers

PMID32908151
PMCPMC7481185
OpenAlexW3084367718

What OpenQuestion holds

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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.