The DOI matches its Crossref record; 112 of the 112 references it cites were found in a registry or an index.
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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In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASES
Cohen, P. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.002321 · Cited by 2,543
Self-citationPhosphorylation-Dephosphorylation of Enzymes
Krebs, E. G., & Beavo, J. A. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004423 · Cited by 2,219
An Adenosine 3′,5′-Monophosphate-dependant Protein Kinase from Rabbit Skeletal Muscle
Walsh, D. A., Perkins, J. P., & Krebs, E. G. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34204-8 · Cited by 1,448
Okadaic acid: a new probe for the study of cellular regulation
Cohen, P., Holmes, C. F. B., & Tsukitani, Y. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90192-e · Cited by 1,373
Self-citationInsulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
Sturgill, T. W., Ray, L. B., ERIKSON, E., & Maller, J. L. (1988) · Nature · doi:10.1038/334715a0 · Cited by 1,017
Embi, N., Rylatt, D. B., & Cohen, P. (1980) · PubMed · Cited by 911
Self-citationEffects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism
Haystead, T., Sim, A. T. R., Carling, D., Honnor, R. C., Tsukitani, Y., Cohen, P., & Hardie, D. G. (1989) · Nature · doi:10.1038/337078a0 · Cited by 838
Self-citationProtein Phosphatases: Properties and Role in Cellular Regulation
Ingebritsen, T. S., & Cohen, P. (1983) · Science · doi:10.1126/science.6306765 · Cited by 645
Self-citationProtein phosphatases come of age
Cohen, P. T. W., & Cohen, P. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88197-6 · Cited by 604
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Flagged first, then by citations
Research works printed but not linked: 2
- Denton, R. M. Adv. Cyclic Nuc. Pmt. Phosph. Res. 20, 293–401 (1986).
- Erikson, E. & Mailer, J. Second Mess. Phosphoproteins 12, 135–143 (1988).
Cited by
Sorted by citations
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Self-citationThe mitogen-activated protein kinase signal transduction pathway
Davis, R. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82362-6 · Cited by 2,112
GSK-3: tricks of the trade for a multi-tasking kinase
Doble, B. W., & Woodgett, J. R. (2003) · Journal of Cell Science · doi:10.1242/jcs.00384 · Cited by 2,084
Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876
Signal Transduction through MAP Kinase Cascades
Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759
Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › 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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