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The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
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Incretins include glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which stimulate insulin secretion post-meals. In type 2 diabetes, GIP's efficacy is reduced, making GLP-1 a viable drug target. GIP originates from preproGIP.
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Insulin receptor-inspired soluble insulin binder.

Christopher Mendoza1, Cameron Hanegan1, Alek Sperry2

  • 1Cell Biology and Physiology, College of Life Sciences, Brigham Young University, Provo, UT, United States.

European Journal of Cell Biology
|February 5, 2023
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Summary

Researchers designed a soluble insulin binder (sIB) that mimics the insulin receptor's (IR) binding site. This new tool effectively reduces insulin signaling in cells, offering a novel way to study insulin's effects.

Keywords:
AKTInsulinInsulin receptor

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Signaling

Background:

  • The insulin receptor (IR) is a key membrane receptor tyrosine kinase mediating insulin's diverse biological actions.
  • Insulin signaling involves IR autophosphorylation and the phosphorylation of intracellular substrates like AKT1.
  • Recent structural insights have revealed the IR's high-affinity insulin binding site, L1.

Purpose of the Study:

  • To design and characterize a simplified, soluble protein that binds insulin.
  • To investigate the potential of this soluble insulin binder (sIB) to interfere with insulin receptor signaling.

Main Methods:

  • Engineering a soluble insulin binder (sIB) by simplifying the IR's L1 binding site.
  • Measuring the binding affinity of sIB to insulin using biochemical assays (Kd = 38 nM).
  • Assessing the impact of sIB on insulin-induced AKT1 and IR autophosphorylation in HEK 293T cells.

Main Results:

  • The engineered sIB, a 17 kDa protein, demonstrated significant binding affinity for insulin.
  • sIB effectively competed with the IR for insulin binding.
  • sIB treatment reduced AKT1 and IR autophosphorylation by over 50% in cellular assays.

Conclusions:

  • The soluble insulin binder (sIB) is a novel protein tool capable of inhibiting insulin receptor signaling.
  • sIB provides a new method for investigating insulin binding and downstream signaling pathways.
  • This research offers a valuable tool for understanding the complexities of insulin action.