ArticleScientific reports2016
β-subunit myristoylation functions as an energy sensor by modulating the dynamics of AMP-activated Protein Kinase.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- AMPK phosphorylation proceeds through hierarchical proteoform cascades revealed by integrated mass spectrometry.Science advances · 2026Article
- Protein lipidation in the tumor microenvironment: enzymology, signaling pathways, and therapeutics.Molecular cancer · 2025Review
- AMPK in Intestinal Health and Disease: A Multifaceted Therapeutic Target for Metabolic and Inflammatory Disorders.Drug design, development and therapy · 2025Review
- The metabolic sensor AMPK: Twelve enzymes in one.Molecular metabolism · 2024Review
- Multiomics analysis identifies oxidative phosphorylation as a cancer vulnerability arising from myristoylation inhibition.Journal of translational medicine · 2024Article
- Mitophagy bridges DNA sensing with metabolic adaption to expand lung cancer stem-like cells.EMBO reports · 2023Article
- DHHC17 Is a New Regulator of AMPK Signaling.Molecular and cellular biology · 2022Article
- Multifaceted Role of AMPK in Viral Infections.Cells · 2021Review
- An AMP-activated protein kinase complex with two distinctive alpha subunits is involved in nutritional stress responses in Trypanosoma cruzi.PLoS neglected tropical diseases · 2021Article
- Operational Experience of an Open-Access, Subscription-Based Mass Spectrometry and Proteomics Facility.Journal of the American Society for Mass Spectrometry · 2018Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heterotrimeric AMP-activated protein kinase (AMPK), consisting of α, β and γ subunits, is a stress-sensing enzyme that is activated by phosphorylation of its activation loop in response to increases in cellular AMP. N-terminal myristoylation of the β-subunit has been shown to suppress Thr172 phosphorylation, keeping AMPK in an inactive state. Here we use amide hydrogen-deuterium exchange mass spectrometry (HDX-MS) to investigate the structural and dynamic properties of the mammalian myristoylated and non-myristoylated inactivated AMPK (D139A) in the presence and absence of nucleotides. HDX MS data suggests that the myristoyl group binds near the first helix of the C-terminal lobe of the kinase domain similar to other kinases. Our data, however, also shows that ATP.Mg
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