Differential activation of insulin receptor substrates 1 and 2 by insulin-like growth factor-activated insulin receptors

Denley, Adam; Carroll, Julie M.; Brierley, Gemma V.; Cosgrove, Leah; Wallace, John; Forbes, Briony; Roberts, Charles T.

doi:10.1128/mcb.01447-06

Cited by 103Growth Hormone and Insulin-like Growth FactorsMetabolism, Diabetes, and CancerFibroblast Growth Factor Research

Differential activation of insulin receptor substrates 1 and 2 by insulin-like growth factor-activated insulin receptors

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Denley, Adam, Carroll, Julie M., Brierley, Gemma V., Cosgrove, Leah, Wallace, John, Forbes, Briony, Roberts, Charles T.·2007·Molecular and Cellular Biology

DOI 10.1128/mcb.01447-06PMC PMC1899985

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Abstract

The insulin-like growth factors (insulin-like growth factor I [IGF-I] and IGF-II) exert important effects on growth, development, and differentiation through the IGF-I receptor (IGF-IR) transmembrane tyrosine kinase. The insulin receptor (IR) is structurally related to the IGF-IR, and at high concentrations, the IGFs can also activate the IR, in spite of their generally low affinity for the latter. Two mechanisms that facilitate cross talk between the IGF ligands and the IR at physiological concentrations have been described. The first of these is the existence of an alternatively spliced IR variant that exhibits high affinity for IGF-II as well as for insulin. A second phenomenon is the ability of hybrid receptors comprised of IGF-IR and IR hemireceptors to bind IGFs, but not insulin. To date, however, direct activation of an IR holoreceptor by IGF-I at physiological levels has not been demonstrated. We have now found that IGF-I can function through both splice variants of the IR, in spite of low affinity, to specifically activate IRS-2 to levels similar to those seen with equivalent concentrations of insulin or IGF-II. The specific activation of IRS-2 by IGF-I through the IR does not result in activation of the extracellular signal-regulated kinase pathway but does induce delayed low-level activation of the phosphatidylinositol 3-kinase pathway and biological effects such as enhanced cell viability and protection from apoptosis. These findings suggest that IGF-I can function directly through the IR and that the observed effects of IGF-I on insulin sensitivity may be the result of direct facilitation of insulin action by IGF-I costimulation of the IR in insulin target tissues.

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The A receptor isoform can stimulate insulin-mediated mitogenesis, even in cells deficient in IGF-I receptors.
“The A receptor isoform can stimulate insulin-mediated mitogenesis, even in cells deficient in IGF-I receptors (50).”
From Diabetes and Cancer (2010) · cites this paper as [50]

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Authors: Denley, A., Carroll, J. M., Brierley, G. V., Cosgrove, L., Wallace, J., Forbes, B., & Roberts, C. T.
Affiliations: Oregon National Primate Research Center (US)
Oregon Health & Science University (US)
Commonwealth Scientific and Industrial Research Organisation (AU)
The University of Adelaide (AU)
Corresponding author: Roberts, Charles T.
ORCID: Carroll, Julie M.
Brierley, Gemma V.
Cosgrove, Leah
Forbes, Briony
Roberts, Charles T.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2007-05-01
Volume: 27
Issue: 10
Pages: 3569-3577
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.01447-06
PMC: PMC1899985
OpenAlex: W2097541712
Cited by: 103
References: 53
Citations by year: 2026: 1 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 3 · 2021: 5 · 2020: 7 · 2019: 4 · 2018: 1 · 2017: 4 · 2016: 5 · 2015: 3 · 2014: 4 · 2013: 7 · 2012: 7
FWCI: 7.58
Type: journal article
Language: en
Update notices: correction (2007-09-01)
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
Funders: Novartis Foundation
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Growth Hormone and Insulin-like Growth Factors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
Keywords: insulin receptor, insulin-like growth factor I, insulin-like growth factor II, insulin receptor substrate 2, IGF-1 receptor, hybrid receptors, receptor cross-talk, phosphatidylinositol 3-kinase signaling, extracellular signal-regulated kinase, apoptosis, cell viability, insulin sensitivity, tyrosine kinase
MeSH terms: Animals, Cell Line, Cell Survival, Humans, Insulin, Insulin-Like Growth Factor I, Insulin-Like Growth Factor II, Phosphoproteins, Receptor, Insulin, Recombinant Fusion Proteins, Signal Transduction, Alternative Splicing, Receptor, IGF Type 1, Insulin-Like Growth Factor Binding Proteins, RNA, Small Interfering, Intracellular Signaling Peptides and Proteins, Mice, Insulin Receptor Substrate Proteins

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Differential activation of insulin receptor substrates 1 and 2 by insulin-like growth factor-activated insulin receptors

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