Evidence map›Paper›PMID 12953116›Full record

ArticleThe Plant cell2003

Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells.

Philippe Giegé, Joshua L Heazlewood, Ute Roessner-Tunali, A Harvey Millar, Alisdair R Fernie, Christopher J Leaver, Lee J Sweetlove

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
7.4field-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

142 citing papers in PubMed, 376 citations in OpenAlex.

  1. Review
  2. ProteinbioRxiv : the preprint server for biology · 2026
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  9. Plastid Transient and Stable Interactions with Other Cell Compartments.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. TheFrontiers in plant science · 2024
    Article
  11. Article
  12. Unique Features of the mInternational journal of molecular sciences · 2023
    Article
  13. Article
  14. Review
  15. Review
  16. Moonlight functions of glycolytic enzymes in cancer.Frontiers in molecular biosciences · 2023
    Review
  17. Review
  18. Article
  19. Article
  20. Article

82 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

7 authors at 5 institutions in 4 countries.

Philippe GiegéInstitut de Biologie Moléculaire des Plantes, Strasbourg 67084, France.
Joshua L Heazlewood
Ute Roessner-Tunali
A Harvey Millar
Alisdair R Fernie
Christopher J Leaver
Lee J Sweetlove
University of Oxford · GBUniversity of Western Australia · AUInstitut de Biologie Moléculaire des Plantes · FRMax Planck Institute of Molecular Plant Physiology · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria fulfill a wide range of metabolic functions in addition to the synthesis of ATP and contain a diverse array of proteins to perform these functions. Here, we present the unexpected discovery of the presence of the enzymes of glycolysis in a mitochondrial fraction of Arabidopsis cells. Proteomic analyses of this mitochondrial fraction revealed the presence of 7 of the 10 enzymes that constitute the glycolytic pathway. Four of these enzymes (glyceraldehyde-3-P dehydrogenase, aldolase, phosphoglycerate mutase, and enolase) were also identified in an intermembrane space/outer mitochondrial membrane fraction. Enzyme activity assays confirmed that the entire glycolytic pathway was present in preparations of isolated Arabidopsis mitochondria, and the sensitivity of these activities to protease treatments indicated that the glycolytic enzymes are present on the outside of the mitochondrion. The association of glycolytic enzymes with mitochondria was confirmed in vivo by the expression of enolase- and aldolase-yellow fluorescent protein fusions in Arabidopsis protoplasts. The yellow fluorescent protein fluorescence signal showed that these two fusion proteins are present throughout the cytosol but are also concentrated in punctate regions that colocalized with the mitochondrion-specific probe Mitotracker Red. Furthermore, when supplied with appropriate cofactors, isolated, intact mitochondria were capable of the metabolism of (13)C-glucose to (13)C-labeled intermediates of the trichloroacetic acid cycle, suggesting that the complete glycolytic sequence is present and active in this subcellular fraction. On the basis of these data, we propose that the entire glycolytic pathway is associated with plant mitochondria by attachment to the cytosolic face of the outer mitochondrial membrane and that this microcompartmentation of glycolysis allows pyruvate to be provided directly to the mitochondrion, where it is used as a respiratory substrate.

Indexed as

GlycolysisArabidopsisArabidopsis ProteinsBacterial ProteinsCarbon RadioisotopesElectrophoresis, Gel, Two-DimensionalEnzymesFructose-Bisphosphate AldolaseFructosediphosphatesGlucoseGlyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating)Luminescent ProteinsMitochondriaPhosphoglycerate MutasePhosphopyruvate HydrataseRecombinant Fusion ProteinsArabidopsis ProteinsBacterial ProteinsCarbon RadioisotopesEnzymesfructose-1,6-diphosphateFructose-Bisphosphate AldolaseFructosediphosphatesGlucoseGlyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating)Luminescent ProteinsPhosphoglycerate MutasePhosphopyruvate HydrataseRecombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID12953116
PMCPMC181336
OpenAlexW2119309660

What Socratic holds

Textmetadata
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 Socratic graph.