AMPK is a direct adenylate charge-regulated protein kinase
Abstract
The adenosine monophosphate (AMP)-activated protein kinase (AMPK) regulates whole-body and cellular energy balance in response to energy demand and supply. AMPK is an αβγ heterotrimer activated by decreasing concentrations of adenosine triphosphate (ATP) and increasing AMP concentrations. AMPK activation depends on phosphorylation of the α catalytic subunit on threonine-172 (Thr(172)) by kinases LKB1 or CaMKKβ, and this is promoted by AMP binding to the γ subunit. AMP sustains activity by inhibiting dephosphorylation of α-Thr(172), whereas ATP promotes dephosphorylation. Adenosine diphosphate (ADP), like AMP, bound to γ sites 1 and 3 and stimulated α-Thr(172) phosphorylation. However, in contrast to AMP, ADP did not directly activate phosphorylated AMPK. In this way, both ADP/ATP and AMP/ATP ratios contribute to AMPK regulation.
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ADP can also activate AMPK.
“but it has been shown that ADP could also activate AMPK (Oakhill et al., 2011)”
From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Oakhill et al., 2011
AMPK functions as a sensor of the cellular adenylate energy charge.
“As such, AMPK functions as a sensor of the cellular adenylate energy charge (84, 85).”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [85]
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- Authors
- Oakhill, J. S., Steel, R., Chen, Z.-P., Scott, J. W., Ling, N., Tam, S., & Kemp, B. E.
- Affiliations
- The University of Melbourne (AU)
- Department of Protein Chemistry and Metabolism, St. Vincent’s Institute of Medical Research, University of Melbourne, 41 Victoria Parade, Fitzroy 3065, Victoria, Australia.
- Corresponding author
- Oakhill, Jonathan S.
- Venue
- Science
- Published
- 2011-06-17
- Volume
- 332
- Issue
- 6036
- Pages
- 1433-1435
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2080107084
- Cited by
- 612
- References
- 27
- Citations by year
- 2026: 25 · 2025: 25 · 2024: 34 · 2023: 27 · 2022: 34 · 2021: 37 · 2020: 34 · 2019: 31 · 2018: 42 · 2017: 51 · 2016: 32 · 2015: 48 · 2014: 52 · 2013: 60 · 2012: 59
- FWCI
- 24.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Research Bank (Australian Catholic University) (submittedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- AMPK, AMPK activation, energy balance, adenosine triphosphate, adenosine diphosphate, AMP, adenosine, Thr172 phosphorylation, LKB1, CaMKKβ, allosteric regulation, kinase regulation
- MeSH terms
- Adenosine Diphosphate, Adenosine Monophosphate, Adenosine Triphosphate, Animals, Binding Sites, Chlorocebus aethiops, Enzyme Activation, Phosphorylation, Recombinant Fusion Proteins, Threonine, Protein Serine-Threonine Kinases, COS Cells, Myristic Acid, Protein Subunits, Calcium-Calmodulin-Dependent Protein Kinase Kinase, AMP-Activated Protein Kinases
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