Arachidonic acid allows SNARE complex formation in the presence of Munc18

Colin Rickman, Bazbek Davletov

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

SNARE complex formation underlies intracellular membrane fusion in eukaryotic organisms; however, the factors regulating the SNARE assembly are not well understood. The neuronal SNARE complex is composed of synaptobrevin2, SNAP-25, and syntaxin1, the latter being under tight control by the cytosolic protein Munc18. We found that the inhibition of syntaxin1 by Munc18 both in nerve terminals and in defined in vitro reactions can be overcome by specific detergents. This serendipitous finding led us to screen biologically relevant fatty acids, revealing that unsaturated arachidonic and linolenic acids can stimulate Munc18-regulated SNARE complex formation in a direct manner. The direct effect of arachidonic acid on the syntaxin1/Munc18 complex suggests a mechanism for the activation of the SNARE assembly pathway and provides a lead for the further investigation of fatty acids that may regulate SNARE-mediated membrane fusion in eukaryotes.
Original languageEnglish
Pages (from-to)545-553
Number of pages9
JournalChemistry and Biology
Volume12
Issue number5
DOIs
Publication statusPublished - May 2005

Keywords

  • Animals
  • Antigens, Surface
  • Arachidonic Acid
  • Detergents
  • Glucosides
  • Munc18 Proteins
  • Nerve Tissue Proteins
  • Octoxynol
  • Rats
  • SNARE Proteins
  • Signal Transduction
  • Synaptic Membranes
  • Synaptosomes
  • Syntaxin 1
  • Vesicular Transport Proteins

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