AMPK: a nutrient and energy sensor that maintains energy homeostasis
Open accessAbstract
AMP-activated protein kinase (AMPK) is a crucial cellular energy sensor. Once activated by falling energy status, it promotes ATP production by increasing the activity or expression of proteins involved in catabolism while conserving ATP by switching off biosynthetic pathways. AMPK also regulates metabolic energy balance at the whole-body level. For example, it mediates the effects of agents acting on the hypothalamus that promote feeding and entrains circadian rhythms of metabolism and feeding behaviour. Finally, recent studies reveal that AMPK conserves ATP levels through the regulation of processes other than metabolism, such as the cell cycle and neuronal membrane excitability.
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Nutrient-sensing pathways such as mTOR and AMPK have a critical role in regulating resilience under chronic stress and malnutrition.
“Nutrient-sensing pathways (for example, mTOR and AMPK) have a critical role in regulating resilience under chronic stress and malnutrition93.”
From Resilience and brain health in global populations (2025) · cites this paper as [93]
The sections on anabolic pathways and AMPK regulation describe AMPK as maintaining energy homeostasis during metabolic stress and regulating TOR-related proteins. They do not establish that mTOR and AMPK regulate resilience under chronic stress and malnutrition; that broader outcome and setting go beyond what the paper says. (LLM, conf=0.84)
Experimental — accuracy not yet measuredTo increase ATP availability, the cells increase the catabolism of energy stores, such as fatty acids, and the biosynthesis of costly fatty acids and ergosterol is decreased.
“To increase ATP availability, the cells increase the catabolism of energy stores, such as fatty acids, and the biosynthesis of”
From Mitochondrial Activity and Cyr1 Are Key Regulators of Ras1 Activation of C. albicans Virulence Pathways (2015) · cites this paper as [55]
The sections on other catabolic pathways and anabolic pathways say AMPK promotes fatty-acid breakdown and reduces ATP-consuming fatty-acid synthesis. The anabolic-pathways section discusses reduced cholesterol synthesis, but does not establish reduced ergosterol synthesis; that specific part of the claim is unsupported by our copy (page numbers unavailable). (LLM, conf=0.87)
Experimental — accuracy not yet measuredIncreased ADP:ATP or AMP:ATP ratios activate AMPK.
“Increased ADP:ATP or AMP:ATP ratios activate AMPK (Hardie et al., 2012)”
From Mitochondrial Dysfunction Induces Senescence with a Distinct Secretory Phenotype (2016) · cites this paper as Hardie et al., 2012
AMP kinase is a known energy sensor that measures ratios of ATP to ADP/AMP and is activated when cellular energy status is low in eukaryotes.
“This activation is not surprising as AMP kinase is a known energy sensor that measures ratios of ATP to ADP/AMP [55] that is activated when cellular energy status is low in eukaryotes.”
From Mitochondrial Activity and Cyr1 Are Key Regulators of Ras1 Activation of C. albicans Virulence Pathways (2015) · cites this paper as [55]
Active AMPK plays a role in the long-term regulation of mitochondrial mass by controlling the transcription and activity of PGC-1α.
“and also plays a role in the long-term regulation of mitochondrial mass by controlling the transcription and activity of PGC-1α [34].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [34]
The α-subunit contains the kinase domain and a critical residue (Thr174 in α1 and Thr172 in α2) that is phosphorylated by upstream kinases.
“The α-subunit contains the kinase domain and a critical residue (Thr174 in α1-subunit and Thr172 in α2-subunit, hereafter referred to as Thr172) that is phosphorylated by upstream kinases [1].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [1]
AMPK activates upon binding with AMP or ADP under conditions of insufficient energy.
“Under conditions of insufficient energy, AMPK activates upon its binding with AMP or adenosine diphosphate (ADP) [1].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [1]
AMPK inhibits by phosphorylation several anabolic enzymes such as ACC, GAPT, HMGCR and GS, affecting glycogen and lipid biosynthesis.
“AMPK inhibits by phosphorylation several anabolic enzymes such as acetyl-coenzyme A (CoA) carboxylase (ACC), glycerol phosphate acyl transferase (GAPT), 3-hydroxyl-3-methylglutaryl CoA reductase (HMGCR) and glycogen synthase (GS) affecting glycogen and lipid biosynthesis”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Hardie et al., 2012
In mammalian cells, fluctuations in cellular energy are monitored by the heterotrimeric AMPK complex.
“In mammalian cells, fluctuations in cellular energy are monitored by the heterotrimeric AMPK complex [reviewed in (83)].”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [83]
AMPK acts as a key metabolic sensor to match energy demand with supply.
“Hence, it acts as a key metabolic sensor to match energy demand with supply (240).”
From Placental Origins of Chronic Disease (2016) · cites this paper as [240]
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Self-citationCBS domains: structure, function, and pathology in human proteins
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Chemical Genetic Screen for AMPKα2 Substrates Uncovers a Network of Proteins Involved in Mitosis
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Self-citation3-Hydroxy-3-methylglutaryl Coenzyme A Reductase
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AMPK functions as an adenylate charge-regulated protein kinase
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Self-citationAMP-activated protein kinase: Also regulated by ADP?
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Self-citationEtoposide Induces ATM-Dependent Mitochondrial Biogenesis through AMPK Activation
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Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase
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Self-citationBateman domains and adenosine derivatives form a binding contract
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ADP Regulates SNF1, the Saccharomyces cerevisiae Homolog of AMP-Activated Protein Kinase
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Self-citationConserved α-Helix Acts as Autoinhibitory Sequence in AMP-activated Protein Kinase α Subunits
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The mechanisms of action of metformin
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“Increased ADP:ATP or AMP:ATP ratios activate AMPK (Hardie et al., 2012), which can induce senescence by phosphorylating p53 (Jones et al.”
BackgroundNutrient-sensing mechanisms and pathways
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The Short Chain Fatty Acid Butyrate Imprints an Antimicrobial Program in Macrophages
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Self-citationGlutathione primes t cell metabolism for inflammation
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AMPK at the Nexus of Energetics and Aging
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Self-citationMolecular mechanism of action of metformin: old or new insights?
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Glucose-regulated phosphorylation of TET2 by AMPK reveals a pathway linking diabetes to cancer
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The molecular targets of resveratrol
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“Upon activation, AMPK diminishes the rates ofmost energy consumingmetabolic programs such as lipid and protein biosynthesis, and triggers energy producing biochemical processes such as lipid oxidation and glycolysis to counter energy depletion [65].”
BackgroundFrom Ancient Pathways to Aging Cells—Connecting Metabolism and Cellular Senescence
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Self-citationOligodendrocyte-Encoded HIF Function Couples Postnatal Myelination and White Matter Angiogenesis
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Metformin Improves Mitochondrial Respiratory Activity through Activation of AMPK
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NAD+ metabolism governs the proinflammatory senescence-associated secretome
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Mechanisms and Regulation of Cellular Senescence
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Extracellular Metabolic Energetics Can Promote Cancer Progression
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Redox control of inflammation in macrophages
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Lipid Metabolism and Ferroptosis
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Systemic pan-AMPK activator MK-8722 improves glucose homeostasis but induces cardiac hypertrophy
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Sestrins inhibit mTORC1 kinase activation through the GATOR complex
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“AMPK activation has multiple effects, including inhibition of gluconeogenesis and adipogenesis [59] that could lead to reduced adiposity.”
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“Lipids are a rich source of ATP, and AMPK induces a lipid catabolic state when ATP levels are low [54,55].”
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- Authors
- Hardie, D. G., Ross, F. A., & Hawley, S. A.
- Affiliations
- University of Dundee (GB)
- Corresponding author
- Hardie, D. Grahame
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2012-03-22
- Volume
- 13
- Issue
- 4
- Pages
- 251-262
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC5726489
- OpenAlex
- W2016752484
- Cited by
- 4,602
- References
- 124
- Citations by year
- 2026: 401 · 2025: 370 · 2024: 275 · 2023: 328 · 2022: 368 · 2021: 406 · 2020: 370 · 2019: 305 · 2018: 302 · 2017: 336 · 2016: 320 · 2015: 293 · 2014: 262 · 2013: 211 · 2012: 50
- FWCI
- 23.83
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Discovery Research Portal (University of Dundee) (acceptedVersion, other-oa)
- Funders
- Wellcome Trust (097726)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- AMPK, energy homeostasis, energy sensing, AMP/ATP ratio, cellular metabolism, catabolism, feeding behaviour, circadian rhythm, hypothalamus, cell cycle regulation, neuronal excitability
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Animals, Appetite, Circadian Rhythm, Energy Metabolism, Glucose, Humans, Hypothalamus, Mammals, Mitochondria, Xenobiotics, Oxidative Stress, Glucose Transporter Type 4, AMP-Activated Protein Kinases
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