Cited by 433Metabolism, Diabetes, and CancerGlycogen Storage Diseases and MyoclonusBiochemical and Molecular Research

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The Glycogen-Binding Domain on the AMPK β Subunit Allows the Kinase to Act as a Glycogen Sensor

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McBride, Andrew, Ghilagaber, Stephanos, Nikolaev, Andrei, Hardie, D. Grahame·2009·Cell Metabolism

DOI 10.1016/j.cmet.2008.11.008PMC PMC2642990

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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.

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Authors: McBride, A., Ghilagaber, S., Nikolaev, A., & Hardie, D. G.
Affiliations: University of Dundee (GB)
Corresponding author: Hardie, D. Grahame
ORCID: Nikolaev, Andrei
Hardie, D. Grahame
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2009-01
Volume: 9
Issue: 1
Pages: 23-34
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2008.11.008
PMC: PMC2642990
OpenAlex: W2123429601
Cited by: 432
References: 40
Citations by year: 2026: 11 · 2025: 17 · 2024: 14 · 2023: 19 · 2022: 18 · 2021: 23 · 2020: 22 · 2019: 19 · 2018: 31 · 2017: 21 · 2016: 28 · 2015: 31 · 2014: 27 · 2013: 28 · 2012: 36
FWCI: 16.26
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/3.0/ (vor, 1657 d)
Locations: Cell Metabolism (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
Funders: Pfizer
AstraZeneca
GlaxoSmithKline
Merck KGaA
Wellcome Trust
European Commission (LSHMCT-2004-005272)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Glycogen Storage Diseases and Myoclonus
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: AMPK, allosteric inhibition, branched oligosaccharides, phosphorylase, energy reserves, kinase regulation, carbohydrate binding
MeSH terms: AMP-Activated Protein Kinase Kinases, Allosteric Regulation, Amino Acid Sequence, Animals, Binding Sites, Cattle, Energy Metabolism, Glycogen, Glycogen Synthase, Molecular Sequence Data, Mutation, Oligosaccharides, Phosphorylation, Mutagenesis, Site-Directed, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Rats, Calcium-Calmodulin-Dependent Protein Kinase Kinase, AMP-Activated Protein Kinases

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The Glycogen-Binding Domain on the AMPK β Subunit Allows the Kinase to Act as a Glycogen Sensor

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