The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle
Abstract
The ability of insulin to promote the phosphorylation of some proteins and the dephosphorylation of others is paradoxical. An insulin-stimulated protein kinase is shown to activate the type-1 protein phosphatase that controls glycogen metabolism, by phosphorylating its regulatory subunit at a specific serine. Furthermore, the phosphorylation of this residue is stimulated by insulin in vivo. Increased and decreased phosphorylation of proteins by insulin can therefore be explained through the same basic underlying mechanism.
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Under anabolic conditions, insulin increases glycogen synthesis by activating glycogen synthase and inhibiting glycogen phosphorylase.
“Under anabolic conditions, insulin augments glycogen synthesis by simultaneously activating glycogen synthase and inhibiting glycogen phosphorylase [148, 149].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [148]
Glycogen synthase is the key insulin-regulated enzyme controlling the rate of muscle glycogen synthesis.
“Glycogen synthase is the key insulin-regulated enzyme that controls the rate of muscle glycogen synthesis [148, 150, 200, 212–214].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [148]
Glycogen synthase exists in active (dephosphorylated) and inactive (phosphorylated) forms.
“Glycogen synthase exists in an active (dephosphorylated) and an inactive (phosphorylated) form [148–150].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [148]
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- Authors
- Dent, P., Lavoinne, A., Nakielny, S., Caudwell, F. B., Watt, P., & Cohen, P.
- Affiliations
- University of Dundee (GB)
- Venue
- Nature
- Published
- 1990-11
- Volume
- 348
- Issue
- 6299
- Pages
- 302-308
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1977182622
- Cited by
- 519
- References
- 112
- Citations by year
- 2025: 2 · 2024: 2 · 2022: 4 · 2021: 2 · 2020: 4 · 2019: 2 · 2018: 6 · 2017: 4 · 2016: 2 · 2015: 5 · 2014: 2 · 2013: 4 · 2012: 5
- FWCI
- 18.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (publishedVersion)
- University of Brighton Repository (University of Brighton) (submittedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
- Keywords
- insulin signaling, glycogen synthesis, skeletal muscle, glycogen phosphorylase, protein phosphatase 1, protein kinases, serine phosphorylation, protein dephosphorylation
- MeSH terms
- Amino Acid Sequence, Animals, Glycogen, Insulin, Kinetics, Models, Biological, Molecular Sequence Data, Muscles, Phosphorylation, Propranolol, Protein Kinases, Rabbits, GTP-Binding Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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