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Related Experiment Videos

The insulin receptor activation process involves localized conformational changes.

V Baron1, P Kaliman, N Gautier

  • 1Institut National de la Santé et de la Recherche Médicale Unité 145, Faculté de Médecine, Nice, France.

The Journal of Biological Chemistry
|November 15, 1992
PubMed
Summary
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Insulin receptor activation involves distinct conformational changes. Ligand binding alters the C-terminus, while autophosphorylation induces broader changes across the beta-subunit, potentially preceding substrate binding.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • The precise molecular mechanism of insulin receptor activation, from ligand binding to substrate phosphorylation, remains incompletely understood.
  • Insulin receptor signaling is crucial for glucose homeostasis and metabolic regulation.

Purpose of the Study:

  • To elucidate the molecular mechanism of insulin receptor signal transduction.
  • To delineate the specific cytoplasmic domains of the insulin receptor beta-subunit involved in activation.
  • To differentiate conformational changes induced by insulin binding versus receptor autophosphorylation.

Main Methods:

  • Utilized antipeptide antibodies targeting specific sequences within the insulin receptor beta-subunit's juxtamembrane, kinase, and C-terminal domains.

Related Experiment Videos

  • Investigated conformational changes in response to insulin binding and receptor autophosphorylation.
  • Examined a kinase-deficient insulin receptor mutant (lysine 1018) to assess hormone-dependent conformational changes.

    • Main Results:

    • Insulin binding induces a conformational change primarily in the beta-subunit C-terminus.
    • Receptor autophosphorylation triggers a distinct and more extensive conformational change affecting the juxtamembrane, kinase, and C-terminal domains.
    • The insulin-induced conformational change occurs independently of kinase activity and may precede autophosphorylation.

    Conclusions:

    • Insulin receptor activation involves sequential conformational alterations.
    • Ligand binding likely induces a transient receptor state facilitating ATP binding and autophosphorylation.
    • Subsequent autophosphorylation-mediated conformational changes are critical for unmasking substrate-binding sites and stabilizing the active receptor conformation.