Evidence map›Paper›PMID 17981998›Full record

ArticleThe Plant cell2007

Glycolytic enzymes associate dynamically with mitochondria in response to respiratory demand and support substrate channeling.

James W A Graham, Thomas C R Williams, Megan Morgan, Alisdair R Fernie, R George Ratcliffe, Lee J Sweetlove

Abstract read
In one paragraph

Article in The Plant cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
–field-weighted citation impact
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

122 citing papers in PubMed.

  1. Review
  2. Article
  3. Identification and Regulation of a Hepatic Lipogenic Metabolon.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Plastid Transient and Stable Interactions with Other Cell Compartments.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Mechanisms and Effects of Substrate Channelling in Enzymatic Cascades.Methods in molecular biology (Clifton, N.J.) · 2022
    Review

62 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

6 authors.

James W A GrahamDepartment of Plant Sciences, University of Oxford, Oxford, OX1 3RB, United Kingdom.
Thomas C R Williams
Megan Morgan
Alisdair R Fernie
R George Ratcliffe
Lee J Sweetlove

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Arabidopsis thaliana, enzymes of glycolysis are present on the surface of mitochondria and free in the cytosol. The functional significance of this dual localization has now been established by demonstrating that the extent of mitochondrial association is dependent on respiration rate in both Arabidopsis cells and potato (Solanum tuberosum) tubers. Thus, inhibition of respiration with KCN led to a proportional decrease in the degree of association, whereas stimulation of respiration by uncoupling, tissue ageing, or overexpression of invertase led to increased mitochondrial association. In all treatments, the total activity of the glycolytic enzymes in the cell was unaltered, indicating that the existing pools of each enzyme repartitioned between the cytosol and the mitochondria. Isotope dilution experiments on isolated mitochondria, using (13)C nuclear magnetic resonance spectroscopy to monitor the impact of unlabeled glycolytic intermediates on the production of downstream intermediates derived from (13)C-labeled precursors, provided direct evidence for the occurrence of variable levels of substrate channeling. Pull-down experiments suggest that interaction with the outer mitochondrial membrane protein, VDAC, anchors glycolytic enzymes to the mitochondrial surface. It appears that glycolytic enzymes associate dynamically with mitochondria to support respiration and that substrate channeling restricts the use of intermediates by competing metabolic pathways.

Indexed as

GlycolysisArabidopsisCell RespirationFructose-Bisphosphate AldolaseMagnetic Resonance SpectroscopyMitochondriaMolecular WeightOxidation-ReductionPentose Phosphate PathwayPlant ProteinsProtein BindingSolanum tuberosumSubstrate SpecificityFructose-Bisphosphate AldolasePlant Proteins

Identifiers

PMID17981998
PMCPMC2174870

What OpenQuestion 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 OpenQuestion graph.