Cited by 146Metabolism, Diabetes, and CancerMuscle metabolism and nutritionAdipose Tissue and Metabolism

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Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism

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Hardie, D. Grahame·2011·Proceedings of the Nutrition Society

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Abstract

The AMP-activated protein kinase (AMPK) is a sensor of cellular energy status, and a regulator of energy balance at both the cellular and whole body levels. Although ubiquitously expressed, its function is best understood in skeletal muscle. AMPK contains sites that reversibly bind AMP or ATP, with an increase in cellular AMP:ATP ratio (signalling a fall in cellular energy status) switching on the kinase. In muscle, AMPK activation is therefore triggered by sustained contraction, and appears to be particularly important in the metabolic changes that occur in the transition from resistance to endurance exercise. Once activated, AMPK switches on catabolic processes that generate ATP, while switching off energy-requiring processes not essential in the short term. Thus, it acutely activates glucose uptake (by promoting translocation of the transporter GLUT4 to the membrane) and fatty acid oxidation, while switching off glycogen synthesis and protein synthesis (the later via inactivation of the mammalian target-of-rapamycin pathway). Prolonged AMPK activation also causes some of the chronic adaptations to endurance exercise, such as increased GLUT4 expression and mitochondrial biogenesis. AMPK contains a glycogen-binding domain that causes a sub-fraction to bind to the surface of the glycogen particle, and it can inhibit glycogen synthesis by phosphorylating glycogen synthase. We have shown that AMPK is inhibited by exposed non-reducing ends in glycogen. We are working on the hypothesis that this ensures that glycogen synthesis is rapidly activated when glycogen becomes depleted after exercise, but is switched off again as soon as glycogen stores are replenished.

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Authors: Hardie, D. G.
Affiliations: University of Dundee (GB)
Corresponding author: Hardie, D. Grahame
ORCID: Hardie, D. Grahame
Venue: Proceedings of the Nutrition Society
Publisher: Cambridge University Press (CUP)
Published: 2010-11-11
Volume: 70
Issue: 1
Pages: 92-99
ISSN: 0029-6651 (ISSN-L)
1475-2719
DOI: 10.1017/s0029665110003915
OpenAlex: W2165667722
Cited by: 146
References: 73
Citations by year: 2026: 4 · 2025: 6 · 2024: 5 · 2023: 5 · 2022: 7 · 2021: 10 · 2020: 4 · 2019: 8 · 2018: 4 · 2017: 10 · 2016: 6 · 2015: 14 · 2014: 15 · 2013: 15 · 2012: 22
FWCI: 1.35
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.cambridge.org/core/terms (unspecified)
Locations: Proceedings of The Nutrition Society (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
Funders: Pfizer
AstraZeneca
University of Dundee
Merck KGaA
Wellcome Trust (080982, 081195)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Keywords: AMPK, energy sensing, skeletal muscle metabolism, endurance exercise, resistance training, GLUT4 translocation, glucose uptake, fatty acid oxidation, glycogen synthesis, glycogen synthase phosphorylation, mTOR signaling, mitochondrial biogenesis, AMP/ATP ratio, exercise adaptation
MeSH terms: Adenosine Monophosphate, Adenosine Triphosphate, Energy Metabolism, Glucose, Glycogen, Humans, Muscle Contraction, Muscle Proteins, Signal Transduction, Exercise, Muscle, Skeletal, Lipid Metabolism, AMP-Activated Protein Kinases

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Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism

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