Studies of the regulated assembly of SNARE complexes in adipocytes

Biochem Soc Trans. 2014 Oct;42(5):1396-400. doi: 10.1042/BST20140114.

Abstract

Insulin plays a fundamental role in whole-body glucose homeostasis. Central to this is the hormone's ability to rapidly stimulate the rate of glucose transport into adipocytes and muscle cells [1]. Upon binding its receptor, insulin stimulates an intracellular signalling cascade that culminates in redistribution of glucose transporter proteins, specifically the GLUT4 isoform, from intracellular stores to the plasma membrane, a process termed 'translocation' [1,2]. This is an example of regulated membrane trafficking [3], a process that also underpins other aspects of physiology in a number of specialized cell types, for example neurotransmission in brain/neurons and release of hormone-containing vesicles from specialized secretory cells such as those found in pancreatic islets. These processes invoke a number of intriguing biological questions as follows. How is the machinery involved in these membrane trafficking events mobilized in response to a stimulus? How do the signalling pathways that detect the external stimulus interface with the trafficking machinery? Recent studies of insulin-stimulated GLUT4 translocation offer insight into such questions. In the present paper, we have reviewed these studies and draw parallels with other regulated trafficking systems.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adipocytes, White / metabolism*
  • Animals
  • Cell Membrane / metabolism*
  • Glucose Transporter Type 4 / chemistry
  • Glucose Transporter Type 4 / metabolism*
  • Humans
  • Insulin / metabolism*
  • Munc18 Proteins / chemistry
  • Munc18 Proteins / metabolism
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Protein Transport
  • Qa-SNARE Proteins / chemistry
  • Qa-SNARE Proteins / metabolism
  • Qb-SNARE Proteins / chemistry
  • Qb-SNARE Proteins / metabolism
  • Qc-SNARE Proteins / chemistry
  • Qc-SNARE Proteins / metabolism
  • Receptor, Insulin / agonists*
  • Receptor, Insulin / metabolism
  • SNARE Proteins / chemistry
  • SNARE Proteins / metabolism*
  • Signal Transduction*
  • Vesicle-Associated Membrane Protein 2 / chemistry
  • Vesicle-Associated Membrane Protein 2 / metabolism

Substances

  • Glucose Transporter Type 4
  • Insulin
  • Munc18 Proteins
  • Qa-SNARE Proteins
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • SNAP23 protein, human
  • SNARE Proteins
  • Slc2a4 protein, mouse
  • VAMP2 protein, human
  • Vesicle-Associated Membrane Protein 2
  • syntaxin 4, human
  • Receptor, Insulin