Evidence map›Paper›PMID 19117544›Full record

ArticleCell metabolism2009

The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor.

Andrew McBride, Stephanos Ghilagaber, Andrei Nikolaev, D Grahame Hardie

Abstract read
In one paragraph

Article in Cell metabolism, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 217 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
217citing papers in PubMed, 1 pooled it
–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

217 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Effects of concurrent training sequence on VOFrontiers in physiology · 2023
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  11. Exercise increases TBC1D1 phosphorylation in human skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2011
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157 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Andrew McBrideDivision of Molecular Physiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.
Stephanos Ghilagaber
Andrei Nikolaev
D Grahame Hardie

Funding

Wellcome Trust
6 · The paper itself

Abstract

AMPK beta subunits contain a conserved domain that causes association with glycogen. Although glycogen availability is known to affect AMPK regulation in vivo, the molecular mechanism for this has not been clear. We now show that AMPK is inhibited by glycogen, particularly preparations with high branching content. We synthesized a series of branched oligosaccharides and show that those with a single alpha1-->6 branch are allosteric inhibitors that also inhibit phosphorylation by upstream kinases. Removal of the outer chains of glycogen using phosphorylase, thus exposing the outer branches, renders inhibition of AMPK more potent. Inhibition by all carbohydrates tested was dependent on the glycogen-binding domain being abolished by mutation of residues required for carbohydrate binding. Our results suggest the hypothesis that AMPK, as well as monitoring immediate energy availability by sensing AMP/ATP, may also be able to sense the status of cellular energy reserves in the form of glycogen.

Indexed as

Allosteric RegulationAmino Acid SequenceAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein Kinase KinaseCattleEnergy MetabolismGlycogenGlycogen SynthaseMolecular Sequence DataMutagenesis, Site-DirectedMutationOligosaccharidesPhosphorylationAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase KinaseGlycogenGlycogen SynthaseOligosaccharidesProtein Serine-Threonine KinasesStk11 protein, rat

Identifiers

PMID19117544
PMCPMC2642990

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.