SNARE zippering

Biosci Rep. 2016 May 6;36(3):e00327. doi: 10.1042/BSR20160004. Print 2016 Jun.

Abstract

SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the stable post-fusion conformation of SNARE complex has been extensively studied with biochemical and biophysical means, the pathway of SNARE zippering has been elusive. In this review, we describe some recent progress in understanding the pathway of SNARE zippering. We particularly focus on the half-zippered intermediate, which is most likely to serve as the main point of regulation by the auxiliary factors.

Keywords: Munc18-1; SNARE; coiled coil; complexin; four-helix bundle; nanodisc; synaptotagmin 1.

Publication types

  • Review
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Humans
  • Membrane Fusion
  • Munc18 Proteins / metabolism
  • Protein Conformation
  • SNARE Proteins / chemistry
  • SNARE Proteins / metabolism*
  • Signal Transduction
  • Synaptotagmin I / metabolism

Substances

  • Munc18 Proteins
  • SNARE Proteins
  • Synaptotagmin I