Tethering the assembly of SNARE complexes

Trends Cell Biol. 2014 Jan;24(1):35-43. doi: 10.1016/j.tcb.2013.09.006. Epub 2013 Oct 9.


The fusion of transport vesicles with their target membranes is fundamental for intracellular membrane trafficking and diverse physiological processes and is driven by the assembly of functional soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes. Prior to fusion, transport vesicles are physically linked to their target membranes by various tethering factors. Recent studies suggest that tethering factors also positively regulate the assembly of functional SNARE complexes, thereby coupling tethering with fusion events. This coupling is mediated, at least in part, by direct physical interactions between tethering factors, SNAREs, and Sec1/Munc18 (SM) proteins. In this review we summarize recent progress in understanding the roles of tethering factors in the assembly of specific and functional SNARE complexes driving membrane-fusion events.

Keywords: SM proteins; SNAREpin; SNAREs; membrane fusion; tethering factors.

Publication types

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

MeSH terms

  • Animals
  • Humans
  • Membrane Fusion
  • Multiprotein Complexes / metabolism
  • Protein Multimerization
  • Protein Subunits / metabolism
  • Protein Transport
  • SNARE Proteins / metabolism*
  • Transport Vesicles / metabolism
  • Vesicular Transport Proteins / metabolism


  • Multiprotein Complexes
  • Protein Subunits
  • SNARE Proteins
  • Vesicular Transport Proteins