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PMID: 1729685 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Carpentier JL, Paccaud JP, Gorden P, Rutter WJ, Orci L

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.

MeSH Terms
Animals Autoradiography CHO Cells Cricetinae DNA Mutational Analysis Down-Regulation Endocytosis Insulin/physiology Phosphoproteins/metabolism Phosphorylation Receptor, Insulin/metabolism Time Factors Transfection
Chemicals
Insulin Phosphoproteins Receptor, Insulin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Carpentier J L
Department of Morphology, University of Geneva Medical Center, Switzerland.
Paccaud J P
Gorden P
Rutter W J
Orci L
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1992-01-01
Pages
162-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC48196
Subset
IM
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