Cited by 904Adipokines, Inflammation, and Metabolic DiseasesCytokine Signaling Pathways and InteractionsUbiquitin and proteasome pathways

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SOCS-1 and SOCS-3 Block Insulin Signaling by Ubiquitin-mediated Degradation of IRS1 and IRS2

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Rui, Liangyou, Yuan, Minsheng, Frantz, Daniel, Shoelson, Steven, White, Morris F.·2002·Journal of Biological Chemistry

DOI 10.1074/jbc.c200444200

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Abstract

Inflammation associates with peripheral insulin resistance, which dysregulates nutrient homeostasis and leads to diabetes. Inflammation induces the expression of SOCS proteins. We show that SOCS1 or SOCS3 targeted IRS1 and IRS2, two critical signaling molecules for insulin action, for ubiquitin-mediated degradation. SOCS1 or SOCS3 bound both recombinant and endogenous IRS1 and IRS2 and promoted their ubiquitination and subsequent degradation in multiple cell types. Mutations in the conserved SOCS box of SOCS1 abrogated its interaction with the elongin BC ubiquitin-ligase complex without affecting its binding to IRS1 or IRS2. The SOCS1 mutants also failed to promote the ubiquitination and degradation of either IRS1 or IRS2. Adenoviral-mediated expression of SOCS1 in mouse liver dramatically reduced hepatic IRS1 and IRS2 protein levels and caused glucose intolerance; by contrast, expression of the SOCS1 mutants had no effect. Thus, SOCS-mediated degradation of IRS proteins, presumably via the elongin BC ubiquitin-ligase, might be a general mechanism of inflammation-induced insulin resistance, providing a target for therapy.

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Authors: Rui, L., Yuan, M., Frantz, D., Shoelson, S., & White, M. F.
Affiliations: Joslin Diabetes Center (US)
Corresponding author: White, Morris F.
ORCID: Rui, Liangyou
Shoelson, Steven
White, Morris F.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2002-11
Volume: 277
Issue: 44
Pages: 42394-42398
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.c200444200
OpenAlex: W2069711307
Cited by: 904
References: 44
Citations by year: 2026: 14 · 2025: 18 · 2024: 18 · 2023: 25 · 2022: 35 · 2021: 39 · 2020: 27 · 2019: 29 · 2018: 42 · 2017: 33 · 2016: 48 · 2015: 27 · 2014: 50 · 2013: 51 · 2012: 57
FWCI: 30.83
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6559 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: SOCS1, SOCS3, IRS-1, insulin receptor substrate 2, insulin signaling, ubiquitin-mediated proteolysis, SOCS box, inflammation, insulin resistance, impaired glucose tolerance, liver, diabetes mellitus
MeSH terms: Suppressor of Cytokine Signaling 1 Protein, Suppressor of Cytokine Signaling 3 Protein, Elongin, Animals, Carrier Proteins, Glucose, Homeostasis, Humans, Insulin Resistance, Male, Mice, Inbred C57BL, Phosphoproteins, Proteins, Repressor Proteins, Transcription Factors, Ubiquitin, Intracellular Signaling Peptides and Proteins, Suppressor of Cytokine Signaling Proteins, Mice, Insulin Receptor Substrate Proteins

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SOCS-1 and SOCS-3 Block Insulin Signaling by Ubiquitin-mediated Degradation of IRS1 and IRS2

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