The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism
Open accessAbstract
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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“Therefore, it comes as no surprise that AMPK is a key mediator of the adaptation to endurance exercise, particularly in skeletal muscle (54).”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [54]
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“Prolonged AMPK activation can lead to a chronic adaptation to endurance exercise, like mitochondrial biogenesis and increased GLUT4 expression [60].”
From Regulation of Energy Substrate Metabolism in Endurance Exercise (2021) · cites this paper as [60]
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The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300
Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., et al. (2003) · Nature · doi:10.1038/nature01705 · Cited by 3,176
AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491
AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy
Hardie, D. G. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2249 · Cited by 2,261
Self-citationMitochondrial dysfunction and type 2 diabetes
Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070
Research works printed but not linked: 1
- Merrill, 1997, AICAR decreases malonyl-CoA and increases fatty acid oxidation in skeletal muscle of the rat, Am J Physiol, 273, E1107
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AMPK activators: mechanisms of action and physiological activities
Kim, J., Yang, G., Kim, Y., Kim, J., & Ha, J. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.16 · Cited by 817
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism
Liemburg-Apers, D. C., Willems, P. H. G. M., Koopman, W. J. H., & Grefte, S. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1520-y · Cited by 412
Jin, Q., Cheng, J. G., Liu, Y., Wu, J. H., Wang, X., Wei, S., Zhou, X., Qin, Z., Jia, J., & Zhen, X. (2014) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2014.03.003 · Cited by 300
White, J. P., Baynes, J. W., Welle, S. L., Kostek, M. C., Matesic, L. E., Sato, S., & Carson, J. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024650 · Cited by 260
“AMPK is activated by low cellular energy status and also muscle contraction [22].”
Metadata
- 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
- 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
- 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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