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Related Concept Videos

Insulin: The Receptor and Signaling Pathways01:28

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Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but...
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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Insulin: Biosynthesis, Chemistry, and Preparation01:25

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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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Insulin Secretory Vesicles01:05

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Insulin secretory vesicles release insulin to stimulate blood glucose uptake and regulate carbohydrate metabolism. When the blood glucose levels increase, glucose enters the pancreatic β-islet cells through glucose transporters. Once inside, glucose is metabolized through glycolysis, the citric acid cycle, and the electron transport chain, producing ATP. This increase in ATP concentration closes ATP-sensitive potassium channels, leading to depolarization of the membrane and the opening of...
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Insulin Formulations: Types and Delivery01:27

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Insulin preparations are categorized by their duration of action into short-acting and long-acting types. Two strategies are used to modify insulin's absorption and pharmacokinetic profile: slowing the absorption post-subcutaneous injection, or altering human insulin's amino acid sequence or protein structure. These changes retain the insulin's ability to bind to the insulin receptor, but alter its behavior in solution or after injection.
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Glucose Homeostasis: Pancreatic Islets and Insulin Secretion01:27

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The pancreatic islets comprising only 1%-2% of the volume are highly vascularized and innervated mini-organs. They contain five endocrine cell types, including β cells that secrete insulin, which is synthesized as a single polypeptide chain, preproinsulin, processed to proinsulin, and finally to insulin and C-peptide. This process is complex and regulated, involving the Golgi complex, the endoplasmic reticulum, and the secretory granules of the β cell.
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Related Experiment Video

Updated: Nov 5, 2025

Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
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Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay

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Understanding insulin and its receptor from their three-dimensional structures.

Michael C Lawrence1

  • 1WEHI, Parkville, Victoria, 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, Victoria, 3050, Australia.

Molecular Metabolism
|May 16, 2021
PubMed
Summary

Single-particle cryo-electron microscopy reveals the atomic details of insulin-receptor interactions, advancing our understanding of this complex system crucial for diabetes treatment.

Keywords:
Cryo-electron microscopyInsulinInsulin receptorProtein structureReceptor tyrosine kinaseX-ray crystallography

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Confocal Imaging of Neuropeptide Y-pHluorin: A Technique to Visualize Insulin Granule Exocytosis in Intact Murine and Human Islets
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Homogeneous Time-resolved Förster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Insulin, discovered 100 years ago, is vital for diabetes treatment but possesses complex molecular structure and receptor interactions.
  • Recent advances in single-particle cryo-electron microscopy (cryo-EM) have significantly enhanced our understanding of insulin-receptor atomic details.

Purpose of the Study:

  • To review the three-dimensional structures of insulin and its receptor.
  • To detail the molecular interactions between insulin and its receptor.
  • To identify current gaps in the structural understanding of the insulin-receptor system.

Main Methods:

  • Review of structural data from single-particle cryo-electron microscopy.
  • Analysis of existing literature on insulin and insulin receptor interactions.

Main Results:

  • A near-complete atomic-level picture of insulin-receptor interactions has been achieved.
  • New insights into the kinetics of insulin-receptor binding have been provided.
  • The extant two-site cross-linking model for hormone-receptor engagement requires revision.

Conclusions:

  • The detailed structural understanding necessitates a revised model of insulin-receptor engagement.
  • Further research is needed to elucidate the initial binding mechanism and the receptor's conformational changes during activation.