AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen
Open accessAbstract
AMP-activated protein kinase (AMPK) is a multisubstrate enzyme activated by increases in AMP during metabolic stress caused by exercise, hypoxia, lack of cell nutrients, as well as hormones, including adiponectin and leptin. Furthermore, metformin and rosiglitazone, frontline drugs used for the treatment of type II diabetes, activate AMPK. Mammalian AMPK is an alphabetagamma heterotrimer with multiple isoforms of each subunit comprising alpha1, alpha2, beta1, beta2, gamma1, gamma2, and gamma3, which have varying tissue and subcellular expression. Mutations in the AMPK gamma subunit cause glycogen storage disease in humans, but the molecular relationship between glycogen and the AMPK/Snf1p kinase subfamily has not been apparent. We show that the AMPK beta subunit contains a functional glycogen binding domain (beta-GBD) that is most closely related to isoamylase domains found in glycogen and starch branching enzymes. Mutation of key glycogen binding residues, predicted by molecular modeling, completely abolished beta-GBD binding to glycogen. AMPK binds to glycogen but retains full activity. Overexpressed AMPK beta1 localized to specific mammalian subcellular structures that corresponded with the expression pattern of glycogen phosphorylase. Glycogen binding provides an architectural link between AMPK and a major cellular energy store and juxtaposes AMPK to glycogen bound phosphatases.
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The CBM is closely related to isoamylase domains found in glycogen and starch branching enzymes.
“The CBM is closely related to isoamylase domains found in glycogen and starch branching enzymes [129].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [129]
The AMPK β subunits contain a central domain, referred to as the carbohydrate-binding motif (CBM) or glycogen-binding domain that allows AMPK to bind to glycogen.
“In regards to AMPK, the AMPK β subunits contain a central domain, referred to as the carbohydrate-binding motif (CBM) or glycogen-binding domain that allows AMPK to bind to glycogen [129].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [129]
The CBM is highly conserved between isoforms and across species, ranging from mammals, fruitfly, worm, yeast, and plants.
“This domain is highly conserved between isoforms and across species, ranging from mammals, fruitfly (Drosophila melanogaster), worm (Caenorhabditis elegans), yeast (Saccharomyces cerevisiae), and plants [129].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [129]
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- Authors
- Polekhina, G., Gupta, A., Michell, B. J., van Denderen, B., Murthy, S., Feil, S. C., Jennings, I. G., Campbell, D. J., Witters, L. A., Parker, M. W., Kemp, B. E., & Stapleton, D.
- Affiliations
- The University of Melbourne (AU)
- Dartmouth College (US)
- Corresponding author
- Stapleton, David
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 13
- Issue
- 10
- Pages
- 867-871
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2027815803
- Cited by
- 423
- References
- 30
- Citations by year
- 2026: 5 · 2025: 9 · 2024: 6 · 2023: 3 · 2022: 14 · 2021: 17 · 2020: 14 · 2019: 12 · 2018: 14 · 2017: 19 · 2016: 19 · 2015: 24 · 2014: 16 · 2013: 22 · 2012: 26
- FWCI
- 9.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3730 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-35712, R01DK035712)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- AMPK, glycogen, glycogen phosphorylase, glycogen storage disease, type 2 diabetes, metformin, rosiglitazone
- MeSH terms
- Amino Acid Sequence, Animals, Glycogen, Glycogen Synthase, Models, Molecular, Molecular Sequence Data, Multienzyme Complexes, Phylogeny, Protein Binding, Stress, Physiological, Gene Expression, Protein Serine-Threonine Kinases, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Protein Subunits, Glycogen Phosphorylase, Rats, AMP-Activated Protein Kinases
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