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Article

Mutation of tyrosine residues 1162 and 1163 of the insulin receptor affects hormone and receptor internalization.

Molecular endocrinology (Baltimore, Md.) - 1 Feb 1990

Reynet C, Caron M, Magré J, Cherqui G, Clauser E, Picard J, Capeau J

Abstract excerpt

Insulin internalization and degradation, insulin receptor internalization and recycling, as well as long term receptor down-regulation were comparatively studied in Chinese hamster ovary (CHO) cell lines, either parental or expressing the wild-type human insulin receptor (CHO.R) or a mutated receptor in which the tyrosine residues in positions 1162 and 1163 were replaced by phenylalanines (CHO.Y2). The two...

Topics

Animals
Cell Line
Cricetinae
Cricetulus
Down-Regulation
Female
Insulin
Mutation
Ovary
Receptor, Insulin
Transduction, Genetic
Transfection

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Tyrosine

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Identifiers

PMID: 2184349
DOI: 10.1210/mend-4-2-304

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2184349-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Mutation of tyrosine residues 1162 and 1163 of the insulin receptor affects hormone and receptor internalization.PMID 2184349Read ↗

Insulin receptor mutation at tyrosines 1162 and 1163 alters both receptor serine phosphorylation and desensitization.Semantic proximity Read ↗

Two naturally occurring mutations in the kinase domain of insulin receptor accelerate degradation of the insulin receptor and impair the kinase activity.Semantic proximity Read ↗

Substitution of isoleucine for methionine at position 1153 in the beta-subunit of the human insulin receptor. A mutation that impairs receptor tyrosine kinase activity, receptor endocytosis, and insulin action.Semantic proximity Read ↗

Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor beta-subunit.Semantic proximity Read ↗

Assessment of the in situ tyrosine kinase activity of mutant insulin receptors lacking tyrosine autophosphorylation sites 1162 and 1163.Semantic proximity Read ↗

Deletion of C-terminal 113 amino acids impairs processing and internalization of human insulin receptor: comparison of receptors expressed in CHO and NIH-3T3 cells.Semantic proximity Read ↗

Internalization of the constitutively active arginine 1152-->glutamine insulin receptor occurs independently of insulin at an accelerated rate.Semantic proximity Read ↗

The insulin receptor with phenylalanine replacing tyrosine-1146 provides evidence for separate signals regulating cellular metabolism and growth.Semantic proximity Read ↗

Characterization of an insulin receptor mutant lacking the subunit processing site.Semantic proximity Read ↗

Two steps of insulin receptor internalization depend on different domains of the beta-subunit.Semantic proximity Read ↗

Insulin inhibition of protein degradation in cells expressing wild-type and mutant insulin receptors.Semantic proximity Read ↗

Decreased phosphorylation of mutant insulin receptor by protein kinase C and protein kinase A.Semantic proximity Read ↗

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