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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.

Biochimica et biophysica acta - 16 Dec 1993

Levy-Toledano R, Accili D, Taylor S I

Abstract excerpt

We have studied the structure and the function of a truncated human insulin receptor in which 113 amino acids (aa 1231-1343) at the C-terminus of the beta-subunit were deleted. In this study, wild-type and truncated insulin receptors were expressed by stable transfection in NIH-3T3 cells and CHO cells. The mutation impairs post-translational processing of the insulin receptor; proteolytic cleavage is retarded,...

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Identifiers

PMID: 8268238
DOI: 10.1016/0167-4889(93)90090-c

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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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.PMID 8268238Read ↗

The insulin receptor functions normally in Chinese hamster ovary cells after truncation of the C terminus.Semantic proximity Read ↗

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

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Characterization of unprocessed insulin proreceptors in COS 7 cells transfected with cDNA with Arg735----Ser735 point mutation at the cleavage site.Semantic proximity Read ↗

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

Effects of amino acid replacements within the tetrabasic cleavage site on the processing of the human insulin receptor precursor expressed in Chinese hamster ovary cells.Semantic proximity Read ↗

Biologic activities of naturally occurring human insulin receptor mutations. Evidence that metabolic effects of insulin can be mediated by a kinase-deficient insulin receptor mutant.Semantic proximity Read ↗

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Normal insulin receptor substrate-1 phosphorylation in autophosphorylation-defective truncated insulin receptor. Evidence that phosphorylation of substrates might be sufficient for certain biological effects evoked by insulin.Semantic proximity Read ↗

Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding.Semantic proximity Read ↗

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