N- to C-terminal SNARE complex assembly promotes rapid membrane fusion

Science. 2006 Aug 4;313(5787):673-6. doi: 10.1126/science.1129486.


Assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) syntaxin 1, SNAP-25, and synaptobrevin 2 is thought to be the driving force for the exocytosis of synaptic vesicles. However, whereas exocytosis is triggered at a millisecond time scale, the SNARE-mediated fusion of liposomes requires hours for completion, which challenges the idea of a key role for SNAREs in the final steps of exocytosis. We found that liposome fusion was dramatically accelerated when a stabilized syntaxin/SNAP-25 acceptor complex was used. Thus, SNAREs do have the capacity to execute fusion at a speed required for neuronal secretion, demonstrating that the maintenance of acceptor complexes is a critical step in biological fusion reactions.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Circular Dichroism
  • Dimerization
  • Exocytosis
  • Liposomes / chemistry*
  • Membrane Fusion*
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Folding
  • Protein Structure, Secondary
  • Qa-SNARE Proteins / chemistry
  • Qa-SNARE Proteins / metabolism*
  • R-SNARE Proteins / chemistry
  • R-SNARE Proteins / metabolism
  • Rats
  • Synaptosomal-Associated Protein 25 / chemistry
  • Synaptosomal-Associated Protein 25 / metabolism*


  • Liposomes
  • Peptide Fragments
  • Qa-SNARE Proteins
  • R-SNARE Proteins
  • Synaptosomal-Associated Protein 25