Cited by 519Metabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase SignalingGlycogen Storage Diseases and Myoclonus

The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle

Dent, Paul, Lavoinne, Alain, Nakielny, Sara, Caudwell, F. Barry, Watt, Peter, Cohen, Philip·1990·Nature

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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Crossref · 10.1038/348302a0

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112 of 112 references verified0 citation errors · 0 not checkable

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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
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

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