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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Southern, P. J., & Berg, P. R. (1982) · PubMed · Cited by 2,740
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Ullrich, A., Bell, J. R., Chen, E. Y., Herrera, R., Petruzzelli, L., Dull, T. J., Gray, A., Coussens, L. M., Liao, Y.-C., Tsubokawa, M., et al. (1985) · Nature · doi:10.1038/313756a0 · Cited by 2,251
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Relief of YY1-induced transcriptional repression by protein-protein interaction with the nucleolar phosphoprotein B23.
Inouye, C. J., & Seto, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37400-8 · Cited by 108
p125Fak Focal Adhesion Kinase Is a Substrate for the Insulin and Insulin-like Growth Factor-I Tyrosine Kinase Receptors
Baron, V. T., Calleja, V., Ferrari, P., Alengrin, F., & OBBERGHEN, E. V. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.7162 · Cited by 108
Effect of Microinjection of a Low-Mr Human Placenta Protein Tyrosine Phosphatase on Induction of Meiotic Cell Division in Xenopus Oocytes
Tonks, N. K., Cicirelli, M. F., Diltz, C. D., Krebs, E. G., & Fischer, E. H. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.2.458 · Cited by 107
A combination of hydrogen peroxide and vanadate concomitantly stimulates protein tyrosine phosphorylation and polyphosphoinositide breakdown in different cell lines
Zick, Y., & Sagi‐Eisenberg, R. (1990) · Biochemistry · doi:10.1021/bi00496a013 · Cited by 107
The insulin receptor with phenylalanine replacing tyrosine-1146 provides evidence for separate signals regulating cellular metabolism and growth.
Wilden, P. A., Backer, J., Kahn, C. R., Cahill, D. A., Schroeder, G. J., & White, M. F. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.9.3358 · Cited by 107
Phosphorylation of Purified Insulin Receptor by cAMP Kinase
Roth, R. A., & Beaudoin, J. D. (1987) · Diabetes · doi:10.2337/diab.36.1.123 · Cited by 106
Self-citation
Site-Directed Perturbation of Protein Kinase C- Integrin Interaction Blocks Carcinoma Cell Chemotaxis
Parsons, M., Epple, M., Kline, A. D., Messent, A., Humphries, M. J., Gilchrist, R., Hart, I. R., Prévostel, C., Hughes, W. E., Parker, P. J., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5897-5911.2002 · Cited by 105
Studies on the autophosphorylation of the insulin receptor from human placenta. Analysis of the sites phosphorylated by two-dimensional peptide mapping
Tavaré, J. M., & Denton, R. M. (1988) · Biochemical Journal · doi:10.1042/bj2520607 · Cited by 105
Structure and expression of rat osteosarcoma (ROS 17/2.8) alkaline phosphatase: product of a single copy gene.
Thiede, M. A., Yoon, K., Golub, I. E., Noda, M., & Rodan, G. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.2.319 · Cited by 105
The transforming and suppressor functions of p53 alleles: effects of mutations that disrupt phosphorylation, oligomerization and nuclear translocation.
Slingerland, J., Jenkins, J. R., & Benchimol, S. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05744.x · Cited by 105
Positive Regulation of Insulin Signaling by Neuraminidase 1
Dridi, L., Seyrantepe, V., Fougerat, A., Pan, X., Bonneil, É., Thibault, P., Moreau, A., Mitchell, G. A., Heveker, N., Cairo, C. W., et al. (2013) · Diabetes · doi:10.2337/db12-1825 · Cited by 106
Hepatic phosphotyrosine phosphatase activity and its alterations in diabetic rats.
Meyerovitch, J., Backer, J., & Kahn, C. R. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114261 · Cited by 104
Relationship of site-specific beta subunit tyrosine autophosphorylation to insulin activation of the insulin receptor (tyrosine) protein kinase activity.
Tornqvist, H. E., & Avruch, J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68823-4 · Cited by 104
Identification of RET Autophosphorylation Sites by Mass Spectrometry
Kawamoto, Y., Takeda, K., Okuno, Y., Yamakawa, Y., Ito, Y., Taguchi, R., Kato, M., Suzuki, H., Takahashi, M., & Nakashima, I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312600200 · Cited by 103
The cysteine-rich domains of the insulin and insulin-like growth factor I receptors are primary determinants of hormone binding specificity. Evidence from receptor chimeras.
Gustafson, T. A., & Rutter, W. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44803-4 · Cited by 103
Self-citation
Functional Properties of Rat Brain Sodium Channels Expressed in a Somatic Cell Line
Scheuer, T., Auld, V. J., Boyd, S. R., Offord, J., Dunn, R., & Catterall, W. A. (1990) · Science · doi:10.1126/science.2154850 · Cited by 103
Functions of the major tyrosine phosphorylation site of the PDGF receptor beta subunit.
Kazlauskas, A., Durden, D. L., & Cooper, J. A. (1991) · Cell Regulation · doi:10.1091/mbc.2.6.413 · Cited by 102
Molecular analysis of the INCENPs (inner centromere proteins): separate domains are required for association with microtubules during interphase and with the central spindle during anaphase.
Mackay, A. M., Eckley, D. M., Chue, C., & Earnshaw, W. C. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.123.2.373 · Cited by 102
The Fps/Fes Protein-Tyrosine Kinase Promotes Angiogenesis in Transgenic Mice
Greer, P. A., Haigh, J. J., Mbamalu, G., Khoo, W., Bernstein, A., & Pawson, T. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6755 · Cited by 102
Identification of the Rat Adapter Grb14 as an Inhibitor of Insulin Actions
Kasus‐Jacobi, A., Perdereau, D., Auzan, C., Clauser, É., OBBERGHEN, E. V., Mauvais‐Jarvis, F., Girard, J. R., & Burnol, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26026 · Cited by 105
Interactions between Two Cytoskeleton-associated Tyrosine Kinases: Calcium-dependent Tyrosine Kinase and Focal Adhesion Tyrosine Kinase
Li, X., Dy, R. C., Cance, W. G., Graves, L. M., & Earp, H. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8917 · Cited by 101
Phosphorylation-site mutagenesis of the growth-associated protein GAP-43 modulates its effects on cell spreading and morphology.
Widmer, F., & Caroni, P. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.120.2.503 · Cited by 101
Vimentin Dephosphorylation by Protein Phosphatase 2A Is Modulated by the Targeting Subunit B55
Turowski, P., Myles, T., Hemmings, B. A., Fernandez, A., & Lamb, N. J. C. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.6.1997 · Cited by 100
Molecular Cloning and Characterization of a Novel Rel/NF-χB Family Member Displaying Structural and Functional Homology to NF-χB p50/p105
Mercurio, F., DiDonato, J. A., Rosette, C., & Karin, M. (1992) · DNA and Cell Biology · doi:10.1089/dna.1992.11.523 · Cited by 100
Properties of a human insulin receptor with a COOH-terminal truncation. I. Insulin binding, autophosphorylation, and endocytosis.
McClain, D. A., Maegawa, H., Levy, J., Huecksteadt, T. P., Dull, T. J., Lee, J., Ullrich, A., & Olefsky, J. M. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68393-0 · Cited by 100
The insulin receptor-related receptor. Tissue expression, ligand binding specificity, and signaling capabilities.
Zhang, B., & Roth, R. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36963-7 · Cited by 100
Self-citation

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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