Tyrosine phosphorylation of the insulin receptor is not required for receptor internalization

Studies in 2,4-dinitrophenol-treated cells

Jonathan M. Backer, C. R. Kahn, M. F. White

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The relation between insulin-stimulated autophosphorylation of the insulin receptor and internalization of the receptor was studied in Fao rat hepatoma cells. Treatment of Fao cells with 2,4-dinitrophenol for 45 min depleted cellular ATP by 80% and equally inhibited insulin-stimulated receptor autophosphorylation, as determined by immunoprecipitation of surface-iodinated or [32P]phosphate-labeled cells with anti-phosphotyrosine antibody. In contrast, internalization of the insulin receptor and internalization and degradation of 125I-labeled insulin by 2,4-dinitrophenol-treated cells were normal. These data show that autophosphorylation of the insulin receptor is not required for the receptor-mediated internalization of insulin in Fao cells and suggest that insulin receptor recycling is independent of autophosphorylation.

Original languageEnglish (US)
Pages (from-to)3209-3213
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number9
StatePublished - 1989
Externally publishedYes

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2,4-Dinitrophenol
Insulin Receptor
Tyrosine
Phosphorylation
Insulin
Phosphotyrosine
Immunoprecipitation
Anti-Idiotypic Antibodies
Hepatocellular Carcinoma
Adenosine Triphosphate
Phosphates

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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abstract = "The relation between insulin-stimulated autophosphorylation of the insulin receptor and internalization of the receptor was studied in Fao rat hepatoma cells. Treatment of Fao cells with 2,4-dinitrophenol for 45 min depleted cellular ATP by 80{\%} and equally inhibited insulin-stimulated receptor autophosphorylation, as determined by immunoprecipitation of surface-iodinated or [32P]phosphate-labeled cells with anti-phosphotyrosine antibody. In contrast, internalization of the insulin receptor and internalization and degradation of 125I-labeled insulin by 2,4-dinitrophenol-treated cells were normal. These data show that autophosphorylation of the insulin receptor is not required for the receptor-mediated internalization of insulin in Fao cells and suggest that insulin receptor recycling is independent of autophosphorylation.",
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