Evidence map›Paper›PMID 12586906›Full record

ArticlePlant physiology2003

In plants, 3-o-methylglucose is phosphorylated by hexokinase but not perceived as a sugar.

Sandra Cortès, Marina Gromova, Adeline Evrard, Claude Roby, Alain Heyraud, Dominique B Rolin, Philippe Raymond, Renaud M Brouquisse

Abstract read
In one paragraph

Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
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  3. Grape ASR Regulates Glucose Transport, Metabolism and Signaling.International journal of molecular sciences · 2022
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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

8 authors.

Sandra CortèsCommissariat à l'Energie Atomique, Centre National de la Recherche Scientifique, Université Joseph Fourier, Unité Mixte de Recherche 5019 Physiologie Cellulaire Végétale, 17 rue des Martyrs, 38054 Grenoble cedex 9, France.
Marina Gromova
Adeline Evrard
Claude Roby
Alain Heyraud
Dominique B Rolin
Philippe Raymond
Renaud M Brouquisse

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, sugars are the main respiratory substrates and important signaling molecules in the regulation of carbon metabolism. Sugar signaling studies suggested that sugar sensing involves several key components, among them hexokinase (HXK). Although the sensing mechanism of HXK is unknown, several experiments support the hypothesis that hexose phosphorylation is a determining factor. Glucose (Glc) analogs transported into cells but not phosphorylated are frequently used to test this hypothesis, among them 3-O-methyl-Glc (3-OMG). The aim of the present work was to investigate the effects and fate of 3-OMG in heterotrophic plant cells. Measurements of respiration rates, protein and metabolite contents, and protease activities and amounts showed that 3-OMG is not a respiratory substrate and does not contribute to biosynthesis. Proteolysis and lipolysis are induced in 3-OMG-fed maize (Zea mays L. cv DEA) roots in the same way as in sugar-starved organs. However, contrary to the generally accepted idea, phosphorous and carbon nuclear magnetic resonance experiments and enzymatic assays prove that 3-OMG is phosphorylated to 3-OMG-6-phosphate, which accumulates in the cells. Insofar as plant HXK is involved in sugar sensing, these findings are discussed on the basis of the kinetic properties because the catalytic efficiency of HXK isolated from maize root tips is five orders of magnitude lower for 3-OMG than for Glc and Man.

Indexed as

Carbohydrate Metabolism3-O-MethylglucoseArabidopsisCarbonCarbon IsotopesCell RespirationEndopeptidasesGlucose-6-PhosphateHexokinaseKineticsMagnetic Resonance SpectroscopyPeptide HydrolasesPhosphorus IsotopesPhosphorylationPlant DevelopmentPlant Proteins3-O-MethylglucoseCarbonCarbon IsotopesEndopeptidasesGlucose-6-PhosphateHexokinasePeptide HydrolasesPhosphorus IsotopesPlant Proteins

Identifiers

PMID12586906
PMCPMC166858

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.