Structure and Physiological Regulation of AMPK
Open accessAbstract
Adenosine monophosphate (AMP)-activated protein kinase (AMPK) is a heterotrimeric αβγ complex that functions as a central regulator of energy homeostasis. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK’s kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs. AMPK senses the cellular energy state by competitive binding of the three adenine nucleotides AMP, ADP, and ATP to three sites in its γ subunit, each, which in turn modulates the activity of AMPK’s kinase domain in its α subunit. Our current understanding of adenine nucleotide binding and the mechanisms by which differential adenine nucleotide occupancies activate or inhibit AMPK activity has been largely informed by crystal structures of AMPK in different activity states. Here we provide an overview of AMPK structures, and how these structures, in combination with biochemical, biophysical, and mutational analyses provide insights into the mechanisms of adenine nucleotide binding and AMPK activity modulation.
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AMPK is a heterotrimeric complex composed of a catalytic α-subunit and β and γ regulatory subunits.
“AMPK, a heterotrimeric complex, is composed of a catalytic α-subunit and beta (β) and gamma (γ) regulatory subunits [19].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [19]
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- Authors
- Yan, Y., Zhou, X. E., Xu, H. E., & Melcher, K.
- Affiliations
- Van Andel Institute (US)
- Corresponding author
- Melcher, Karsten
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2018-11-09
- Volume
- 19
- Issue
- 11
- Pages
- 3534
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6274893
- OpenAlex
- W2900317655
- Cited by
- 254
- References
- 65
- Citations by year
- 2026: 31 · 2025: 44 · 2024: 43 · 2023: 37 · 2022: 45 · 2021: 31 · 2020: 17 · 2019: 6
- FWCI
- 1.32
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (GM129436)
- 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, energy homeostasis, adenine nucleotide binding, AMPK activation, AMPK inhibition, gamma subunit, AMP/ATP ratio, kinase domain, crystal structure, allosteric regulation, catabolic pathways
- MeSH terms
- Allosteric Regulation, Animals, Disease, Energy Metabolism, Humans, Models, Molecular, Phosphorylation, AMP-Activated Protein Kinases
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