Membrane fusion: SNAREs and regulation

Cell Mol Life Sci. 2008 Sep;65(18):2814-32. doi: 10.1007/s00018-008-8352-3.


SNARE (SNAP receptor) proteins drive intracellular membrane fusion and contribute specificity to membrane trafficking. The formation of SNAREpins between membranes is spatially and temporally controlled by a network of sequentially acting accessory components. These regulators add an additional layer of specificity, arrest SNAREpin intermediates, lower the energy required for fusion, and couple membrane fusion to triggering signals. The functional activity of some of these regulators determines the plasticity of regulated exocytosis.

Publication types

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

MeSH terms

  • Animals
  • Exocytosis / physiology
  • Humans
  • Membrane Fusion / physiology*
  • Munc18 Proteins / metabolism
  • Nerve Tissue Proteins / metabolism
  • Q-SNARE Proteins / metabolism
  • R-SNARE Proteins / metabolism
  • SNARE Proteins / chemistry
  • SNARE Proteins / metabolism*
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins / metabolism
  • Synaptotagmins / metabolism
  • Transport Vesicles / metabolism


  • Munc18 Proteins
  • Nerve Tissue Proteins
  • Q-SNARE Proteins
  • R-SNARE Proteins
  • SNARE Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Synaptotagmins