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Related Experiment Videos

Insulin receptor internalization and signalling

G M Di Guglielmo1, P G Drake, P C Baass

  • 1Department of Biochemistry, McGill University, Montreal, Quebec, Canada.

Molecular and Cellular Biochemistry
|June 3, 1998
PubMed
Summary
This summary is machine-generated.

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Insulin receptor kinase (IRK) activation and signaling occur within endosomes, not just the cell surface. This internalization process is crucial for insulin clearance and regulating insulin sensitivity.

Area of Science:

  • Cell Biology
  • Endocrinology
  • Signal Transduction

Background:

  • Insulin receptor kinase (IRK) activation is vital for insulin signaling.
  • Insulin binding triggers rapid internalization of insulin-IRK complexes into endosomes (EN).
  • Endosomal insulin uptake contributes to insulin clearance and IRK downregulation.

Purpose of the Study:

  • To investigate the role of endosomal insulin receptor kinase activation in insulin signaling.
  • To identify the primary site of insulin-stimulated IRS-1 phosphorylation and PI3K activation.
  • To explore mechanisms regulating IRK activity within endosomes.

Main Methods:

  • In vivo rat liver model with exclusive endosomal IRK activation.
  • Studies using isolated rat adipocytes.

Related Experiment Videos

  • Identification of endosomal acidic insulinase and associated phosphotyrosine phosphatase(s).

    • Main Results:

    • Endosomal IRKs exclusively activate IRS-1 tyrosine phosphorylation and induce hypoglycemia.
    • Endosomes are the principal site of insulin-stimulated IRS-1 tyrosine phosphorylation and PI3K activation.
    • Endosomes contain an acidic insulinase limiting IRK activation and phosphotyrosine phosphatase(s) regulating IRK activity.

    Conclusions:

    • Insulin-mediated internalization of IRKs into endosomes is critical for signal transduction.
    • Endosomal localization regulates IRK activity, insulin signaling, and insulin levels.
    • Endosomal processing impacts insulin sensitivity and cellular IRK concentration.