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. 1992 Jan 1;89(1):162–166. doi: 10.1073/pnas.89.1.162

Insulin-induced surface redistribution regulates internalization of the insulin receptor and requires its autophosphorylation.

J L Carpentier 1, J P Paccaud 1, P Gorden 1, W J Rutter 1, L Orci 1
PMCID: PMC48196  PMID: 1729685

Abstract

The role of insulin-induced receptor autophosphorylation in its internalization was analyzed by comparing 125I-labeled insulin (125I-insulin) internalization in Chinese hamster ovary (CHO) cell lines transfected with normal (CHO.T) or mutated insulin receptors. In four cell lines with a defect of insulin-induced autophosphorylation, 125I-insulin internalization was impaired. By contrast, in CHO.T cells and in two other CHO cell lines with amino acid deletions or insertions that do not perturb autophosphorylation, 125I-insulin internalization was not affected. A morphological analysis showed that the inhibition is linked to the ligand-specific surface redistribution in which the insulin-receptor complexes leave microvilli and concentrate on nonvillous segments of the membrane where endocytosis occurs.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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