Cited by 1,070Metabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase SignalingPancreatic function and diabetes

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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

Ellis, Leland, Clauser, Eric, Morgan, David O., Edery, Marc, Roth, Richard A., Rutter, William J.·1986·Cell

DOI 10.1016/0092-8674(86)90786-5

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Abstract

Insulin stimulates the autophosphorylation of tyrosine residues of the beta subunit of the insulin receptor (IR); this modified insulin-independent kinase has increased activity toward exogenous substrates in vitro. We show here that replacement of one or both of the twin tyrosines (residues 1162 and 1163) with phenylalanine results in a dramatic reduction in or loss of insulin-activated autophosphorylation and kinase activity in vitro. In vivo, these mutations not only result in a substantial decrease in insulin-stimulated IR autophosphorylation but also in a parallel decrease in the insulin-activated uptake of 2-deoxyglucose. Furthermore, a truncated IR protein (lacking the last 112 amino acids) has an unstable beta subunit; this mutant has no kinase activity in vitro or in vivo and does not mediate insulin-stimulated uptake of 2-deoxyglucose. IR autophosphorylation is thus implicated in the regulation of IR activities, with tyrosines 1162 and 1163 as major sites of this regulation.

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Untitled work
Drexler, H. (2002) · doi:10.1290/1071-2690(2002)038

Authors: Ellis, L., Clauser, E., Morgan, D. O., Edery, M., Roth, R. A., & Rutter, W. J.
Affiliations: University of California, San Francisco (US)
Stanford University (US)
ORCID: Morgan, David O.
Roth, Richard A.
Venue: Cell
Publisher: Elsevier BV
Published: 1986-06
Volume: 45
Issue: 5
Pages: 721-732
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(86)90786-5
OpenAlex: W2030156849
Cited by: 1,070
References: 57
Citations by year: 2026: 1 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 4 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 4 · 2015: 6 · 2014: 4 · 2013: 1 · 2012: 5
FWCI: 34.23
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01am021344-09, 5r01am034926-02)
National Institute of General Medical Sciences (GM 28520)
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 › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
Keywords: insulin receptor, insulin receptor beta-subunit, autophosphorylation, 2-deoxyglucose uptake, insulin signaling, point mutations
MeSH terms: Amino Acid Sequence, Animals, Cell Line, Cricetulus, Deoxy Sugars, Deoxyglucose, DNA, Female, Gene Expression Regulation, Cricetinae, Humans, Insulin, Ovary, Phosphorylation, Protein-Tyrosine Kinases, Receptor, Insulin, Transfection, Tyrosine

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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose

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