Insulin-induced surface redistribution regulates internalization of the insulin receptor and requires its autophosphorylation
- Univ. of Geneva (Switzerland)
- National Inst. of Health, Bethesda, MD (United States)
- Univ. of California, San Francisco (United States)
The role of insulin-induced receptor autophosphorylation in its internalization was analyzed by comparing {sup 125}I-labeled insulin ({sup 125}I-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, {sup 125}I-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, {sup 125}I-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.
- OSTI ID:
- 5618004
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 89:1; ISSN 0027-8424; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ANIMAL CELLS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
CHEMICAL REACTIONS
CHO CELLS
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
HORMONES
INSULIN
INTERMEDIATE MASS NUCLEI
INTERNAL CONVERSION RADIOISOTOPES
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
MEMBRANE PROTEINS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PEPTIDE HORMONES
PHOSPHORYLATION
PROTEINS
RADIOISOTOPES
RADIORECEPTOR ASSAY
RECEPTORS
TRACER TECHNIQUES
UPTAKE