ArticleThe Journal of biological chemistry2015
The recruitment of AMP-activated protein kinase to glycogen is regulated by autophosphorylation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- AMPK phosphorylation proceeds through hierarchical proteoform cascades revealed by integrated mass spectrometry.Science advances · 2026Article
- Does AMPK bind glycogen in skeletal muscle or is the relationship correlative?Essays in biochemistry · 2024Review
- Noncanonical PDK4 action alters mitochondrial dynamics to affect the cellular respiratory status.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Post-translational Modifications: The Signals at the Intersection of Exercise, Glucose Uptake, and Insulin Sensitivity.Endocrine reviews · 2022Review
- Role of AMPK in autophagy.Frontiers in physiology · 2022Review
- Demystifying Chronic Kidney Disease of Unknown Etiology (CKDu): Computational Interaction Analysis of Pesticides and Metabolites with Vital Renal Enzymes.Biomolecules · 2021Article
- Post-Translational Modifications of the Energy Guardian AMP-Activated Protein Kinase.International journal of molecular sciences · 2021Review
- AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy.Nature communications · 2020Article
- Reciprocal Association between the Apical Junctional Complex and AMPK: A Promising Therapeutic Target for Epithelial/Endothelial Barrier Function?International journal of molecular sciences · 2019Review
- Cyclin-dependent kinase 1-mediated AMPK phosphorylation regulates chromosome alignment and mitotic progression.Journal of cell science · 2019Article
- Structures of AMP-activated protein kinase bound to novel pharmacological activators in phosphorylated, non-phosphorylated, and nucleotide-free states.The Journal of biological chemistry · 2019Article
- Conformational heterogeneity of the allosteric drug and metabolite (ADaM) site in AMP-activated protein kinase (AMPK).The Journal of biological chemistry · 2018Article
- Interactive Roles for AMPK and Glycogen from Cellular Energy Sensing to Exercise Metabolism.International journal of molecular sciences · 2018Review
- Exercise-induced molecular mechanisms promoting glycogen supercompensation in human skeletal muscle.Molecular metabolism · 2018Article
- Implications of AMPK in the Formation of Epithelial Tight Junctions.International journal of molecular sciences · 2018Review
- Relationship between genetic variation at PPP1R3B and levels of liver glycogen and triglyceride.Hepatology (Baltimore, Md.) · 2018Article
- AMPK in skeletal muscle function and metabolism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Review
- 2-Arachidonoylglycerol ameliorates inflammatory stress-induced insulin resistance in cardiomyocytes.The Journal of biological chemistry · 2017Article
- Exercise-stimulated glucose uptake - regulation and implications for glycaemic control.Nature reviews. Endocrinology · 2017Review
- Mesenchymal Stromal Cells Accelerate Epithelial Tight Junction Assembly via the AMP-Activated Protein Kinase Pathway, Independently of Liver Kinase B1.Stem cells international · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian AMP-activated protein kinase (AMPK) is an obligatory αβγ heterotrimeric complex carrying a carbohydrate-binding module (CBM) in the β-subunit (AMPKβ) capable of attaching AMPK to glycogen. Nonetheless, AMPK localizes at many different cellular compartments, implying the existence of mechanisms that prevent AMPK from glycogen binding. Cell-free carbohydrate binding assays revealed that AMPK autophosphorylation abolished its carbohydrate-binding capacity. X-ray structural data of the CBM displays the central positioning of threonine 148 within the binding pocket. Substitution of Thr-148 for a phospho-mimicking aspartate (T148D) prevents AMPK from binding to carbohydrate. Overexpression of isolated CBM or β1-containing AMPK in cellular models revealed that wild type (WT) localizes to glycogen particles, whereas T148D shows a diffuse pattern. Pharmacological AMPK activation and glycogen degradation by glucose deprivation but not forskolin enhanced cellular Thr-148 phosphorylation. Cellular glycogen content was higher if pharmacological AMPK activation was combined with overexpression of T148D mutant relative to WT AMPK. In summary, these data show that glycogen-binding capacity of AMPKβ is regulated by Thr-148 autophosphorylation with likely implications in the regulation of glycogen turnover. The findings further raise the possibility of regulated carbohydrate-binding function in a wider variety of CBM-containing proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.