Identification of IRS-1 Ser-1101 as a target of S6K1 in nutrient- and obesity-induced insulin resistance
Open accessAbstract
S6K1 has emerged as a critical signaling component in the development of insulin resistance through phosphorylation and inhibition of IRS-1 function. This effect can be triggered directly by nutrients such as amino acids or by insulin through a homeostatic negative-feedback loop. However, the role of S6K1 in mediating IRS-1 phosphorylation in a physiological setting of nutrient overload is unresolved. Here we show that S6K1 directly phosphorylates IRS-1 Ser-1101 in vitro in the C-terminal domain of the protein and that mutation of this site largely blocks the ability of amino acids to suppress IRS-1 tyrosine and Akt phosphorylation. Consistent with this finding, phosphorylation of IRS-1 Ser-1101 is increased in the liver of obese db/db and wild-type, but not S6K1 −/− , mice maintained on a high-fat diet and is blocked by siRNA knockdown of S6K1 protein. Finally, infusion of amino acids in humans leads to the concomitant activation of S6K1, phosphorylation of IRS-1 Ser-1101, a reduction in IRS-1 function, and insulin resistance in skeletal muscle. These findings indicate that nutrient- and hormonal-dependent activation of S6K1 causes insulin resistance in mice and humans, in part, by mediating IRS-1 Ser-1101 phosphorylation.
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S6K phosphorylation of IRS1 at S1101 is increased in genetic and diet-induced obese mice and has shown to induce insulin resistance.
“S6K phosphorylation of IRS1 at S1101 is increased in genetic and diet-induced obese mice and has shown to induce insulin resistance [154].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [154]
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- Authors
- Tremblay, F., Brûlé, S., Hee Um, S., Li, Y., Masuda, K., Roden, M., Sun, X. J., Krebs, M., Polakiewicz, R. D., Thomas, G., & Marette, A.
- Affiliations
- Université Laval (CA)
- Genome Research Institute, University of Cincinnati, Cincinnati, OH 45237;
- Cell Signaling Technology (United States) (US)
- University of Cincinnati (US)
- Hanusch Hospital (AT)
- University of Chicago (US)
- Medical University of Vienna (AT)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-08-28
- Volume
- 104
- Issue
- 35
- Pages
- 14056-14061
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1950339
- OpenAlex
- W2078281362
- Cited by
- 465
- References
- 48
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 13 · 2023: 19 · 2022: 21 · 2021: 24 · 2020: 26 · 2019: 22 · 2018: 23 · 2017: 23 · 2016: 33 · 2015: 32 · 2014: 22 · 2013: 33 · 2012: 39
- FWCI
- 9.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Foundation for the Study of Diabetes
- Novo Nordisk
- Österreichische Diabetes Gesellschaft
- National Institutes of Health
- Canadian Institutes of Health Research
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK73802, R01DK073802)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Keywords
- IRS-1, S6K1, insulin resistance, obesity, high-fat diet, amino acids, nutrient signaling, Akt phosphorylation, db/db mice, skeletal muscle, liver, mTOR signaling
- MeSH terms
- Animals, Humans, Insulin Resistance, Nutritional Status, Obesity, Phosphoproteins, Phosphorylation, RNA, Messenger, Serine, Sirolimus, RNA, Small Interfering, Mice, Insulin Receptor Substrate Proteins
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