A common mechanism for the regulation of vesicular SNAREs on phospholipid membranes

Kuang Hu, Colin Rickman, Joe Carroll, Bazbek Davletov

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


The SNARE (soluble N -ethylmaleimide-sensitive fusion protein attachment protein receptor) family of proteins is essential for membrane fusion in intracellular traffic in eukaryotic organisms. v-SNAREs (vesicular SNAREs) must engage target SNAREs in the opposing membrane to form the fusogenic SNARE complex. Temporal and spatial control of membrane fusion is important for many aspects of cell physiology and may involve the regulation of the SNAREs resident on intracellular membranes. Here we show that the v-SNARE synaptobrevin 2, also known as VAMP (vesicle-associated membrane protein) 2, is restricted from forming the SNARE complex in chromaffin granules from adrenal medullae to the same degree as in brain-purified synaptic vesicles. Our analysis indicates that the previously reported synaptophysin-synaptobrevin interaction is not likely to be involved in regulation of the v-SNARE. Indeed, the restriction can be reproduced for two distinct v-SNARE homologues, synaptobrevin 2 and cellubrevin/VAMP3, by reconstituting them in pure liposomal membranes. Overall, our data uncover a common mechanism for the control of SNARE engagement where intact phospholipid membranes rather than proteins down-regulate vesicular SNAREs in different cellular organelles.
Original languageEnglish
Pages (from-to)781-785
Number of pages5
JournalBiochemical Journal
Issue number3
Publication statusPublished - 1 Feb 2004


  • Animals
  • Brain
  • Carrier Proteins
  • Cattle
  • Chromaffin Granules
  • Lipid Bilayers
  • Liposomes
  • Membrane Proteins
  • Phospholipids
  • R-SNARE Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Synaptic Vesicles
  • Synaptophysin
  • Vesicular Transport Proteins


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