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Intermolecular phosphorylation between insulin holoreceptors does not stimulate substrate kinase activity

J Lee1, S E Shoelson, P F Pilch

  • 1Department of Biochemistry, Boston University, School of Medicine, Massachusetts 02118, USA.

The Journal of Biological Chemistry
|December 29, 1995
PubMed
Summary

Researchers created a new insulin analog to study insulin receptor interactions. Inter-receptor phosphorylation was observed but did not activate the receptor, suggesting it

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • Insulin receptors (IR) mediate insulin's metabolic and mitogenic effects.
  • IR activation involves autophosphorylation and subsequent substrate phosphorylation.
  • The role of intermolecular phosphorylation in IR activation remains unclear.

Purpose of the Study:

  • To investigate the role of intermolecular insulin receptor phosphorylation in receptor activation.
  • To determine if phosphorylation between insulin receptors can activate substrate receptors.

Main Methods:

  • Photocoupling of a biotinylated insulin analog (BBpa-insulin) to native insulin receptors.
  • Utilizing BBpa-insulin-bound, autophosphorylated receptors to phosphorylate substrate receptors.
  • Assessing substrate receptor phosphorylation and activation status.

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Main Results:

  • A uniform population of insulin receptors with covalently bound ligand was generated.
  • Inter-receptor phosphorylation of substrate receptors occurred, reaching 50% of maximal autophosphorylation.
  • This intermolecular phosphorylation did not significantly activate the substrate receptor.

Conclusions:

  • Intermolecular phosphorylation of insulin holoreceptors is not a significant activation mechanism.
  • Insulin receptor activation likely relies on intramolecular autophosphorylation.
  • This finding clarifies a potential signaling pathway in insulin action.