Cited by 132Metabolism, Diabetes, and CancerGlycogen Storage Diseases and MyoclonusBiochemical and Molecular Research

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AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase

Bultot, Laurent, Guigas, Bruno, Von Wilamowitz-Moellendorff, Alexander, Maisin, Liliane, Vertommen, Didier, Hussain, Nusrat, Beullens, Monique, Guinovart, Joan J., Foretz, Marc, Viollet, Benoît, Sakamoto, Kei, Hue, Louis, Rider, Mark H.·2012·Biochemical Journal

DOI 10.1042/bj20112026

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Abstract

Recombinant muscle GYS1 (glycogen synthase 1) and recombinant liver GYS2 were phosphorylated by recombinant AMPK (AMP-activated protein kinase) in a time-dependent manner and to a similar stoichiometry. The phosphorylation site in GYS2 was identified as Ser7, which lies in a favourable consensus for phosphorylation by AMPK. Phosphorylation of GYS1 or GYS2 by AMPK led to enzyme inactivation by decreasing the affinity for both UDP-Glc (UDP-glucose) [assayed in the absence of Glc-6-P (glucose-6-phosphate)] and Glc-6-P (assayed at low UDP-Glc concentrations). Incubation of freshly isolated rat hepatocytes with the pharmacological AMPK activators AICA riboside (5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside) or A769662 led to persistent GYS inactivation and Ser7 phosphorylation, whereas inactivation by glucagon treatment was transient. In hepatocytes from mice harbouring a liver-specific deletion of the AMPK catalytic α1/α2 subunits, GYS2 inactivation by AICA riboside and A769662 was blunted, whereas inactivation by glucagon was unaffected. The results suggest that GYS inactivation by AMPK activators in hepatocytes is due to GYS2 Ser7 phosphorylation.

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Authors: Bultot, L., Guigas, B., Von Wilamowitz-Moellendorff, A., Maisin, L., Vertommen, D., Hussain, N., Beullens, M., Guinovart, J. J., Foretz, M., Viollet, B., Sakamoto, K., Hue, L., & Rider, M. H.
Affiliations: de Duve Institute (BE)
Leiden University Medical Center (NL)
MRC Protein Phosphorylation Unit, Sir James Black Centre, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
KU Leuven (BE)
Institute for Research in Biomedicine (ES)
Centre National de la Recherche Scientifique (FR)
INSERM U1016, Institut Cochin, CNRS UMR8104, Université Paris Descartes, Sorbonne Paris Cité, Paris 75014, France
University of Dundee (GB)
Corresponding author: Bultot, Laurent
Maisin, Liliane
Vertommen, Didier
Hussain, Nusrat
Hue, Louis
ORCID: Bultot, Laurent
Guigas, Bruno
Vertommen, Didier
Beullens, Monique
Guinovart, Joan J.
Foretz, Marc
Sakamoto, Kei
Rider, Mark H.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2012-03-14
Volume: 443
Issue: 1
Pages: 193-203
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20112026
OpenAlex: W2075032036
Cited by: 131
References: 54
Citations by year: 2026: 10 · 2025: 6 · 2024: 8 · 2023: 9 · 2022: 10 · 2021: 9 · 2020: 9 · 2019: 11 · 2018: 5 · 2017: 13 · 2016: 8 · 2015: 13 · 2014: 4 · 2013: 10 · 2012: 5
FWCI: 4.10
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Journal (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (publishedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Leiden Repository (Leiden University) (submittedVersion)
DIAL (Catholic University of Leuven) (submittedVersion)
Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion)
Lirias (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Glycogen Storage Diseases and Myoclonus
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: AMPK, glycogen synthase, glycogen synthase 1, enzyme inactivation, liver glycogen metabolism, hepatocytes, AICA riboside, A769662, glucagon, UDP-glucose, glucose-6-phosphate
MeSH terms: Amino Acid Sequence, Aminoimidazole Carboxamide, Animals, Biphenyl Compounds, Cells, Cultured, Enzyme Activation, Glycogen Synthase, Humans, Liver, Male, Phosphorylation, Protein Processing, Post-Translational, Pyrones, Ribonucleotides, Thiophenes, Consensus Sequence, Rats, Wistar, Cyclic AMP-Dependent Protein Kinases, Mice, Knockout, Apraxia, Ideomotor, Enzyme Activators, Hepatocytes, Mice, Rats, AMP-Activated Protein Kinases

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AMP-activated protein kinase phosphorylates and inactivates liver glycogen synthase

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