SNAP receptors implicated in vesicle targeting and fusion

Nature. 1993 Mar 25;362(6418):318-24. doi: 10.1038/362318a0.


The N-ethylmaleimide-sensitive fusion protein (NSF) and the soluble NSF attachment proteins (SNAPs) appear to be essential components of the intracellular membrane fusion apparatus. An affinity purification procedure based on the natural binding of these proteins to their targets was used to isolate SNAP receptors (SNAREs) from bovine brain. Remarkably, the four principal proteins isolated were all proteins associated with the synapse, with one type located in the synaptic vesicle and another in the plasma membrane, suggesting a simple mechanism for vesicle docking. The existence of numerous SNARE-related proteins, each apparently specific for a single kind of vesicle or target membrane, indicates that NSF and SNAPs may be universal components of a vesicle fusion apparatus common to both constitutive and regulated fusion (including neurotransmitter release), in which the SNAREs may help to ensure vesicle-to-target specificity.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Brain / physiology*
  • Carrier Proteins / physiology*
  • Cattle
  • Cell Membrane / physiology
  • Hydrolysis
  • Membrane Fusion*
  • Membrane Proteins*
  • Models, Biological
  • Molecular Sequence Data
  • N-Ethylmaleimide-Sensitive Proteins
  • Nerve Tissue Proteins / physiology
  • Synaptic Vesicles / physiology
  • Synaptosomal-Associated Protein 25
  • Vesicular Transport Proteins*


  • Carrier Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Synaptosomal-Associated Protein 25
  • Vesicular Transport Proteins
  • Adenosine Triphosphate
  • N-Ethylmaleimide-Sensitive Proteins