Studies of the regulated assembly of SNARE complexes in adipocytes

Dimitrios Kioumourtzoglou, Jessica B.A. Sadler, Hannah L. Black, Rebecca Berends, Cassie Wellburn, Nia J. Bryant, Gwyn W. Gould*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

7 Citations (Scopus)

Abstract

Insulin plays a fundamental role inwhole-body glucose homeostasis. Central to this is the hormone's ability to rapidly stimulate the rate of glucose transport into adipocytes andmuscle 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.

Original languageEnglish
Pages (from-to)1396-1400
Number of pages5
JournalBiochemical Society Transactions
Volume42
Issue number5
DOIs
Publication statusPublished - 31 Oct 2014

Keywords

  • insulin
  • membrane fusion
  • phosphorylation
  • Sec1/Munc18 protein
  • soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE)

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