A cascade of multiple proteins and lipids catalyzes membrane fusion

Mol Biol Cell. 2017 Mar 15;28(6):707-711. doi: 10.1091/mbc.E16-07-0517.

Abstract

Recent studies suggest revisions to the SNARE paradigm of membrane fusion. Membrane tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE assembly into trans-complexes. SNARE-domain zippering draws the bilayers into immediate apposition and provides a platform to position fusion triggers such as Sec 17/α-SNAP and/or synaptotagmin, which insert their apolar "wedge" domains into the bilayers, initiating the lipid rearrangements of fusion.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Lipids
  • Membrane Fusion / physiology
  • Membrane Proteins / metabolism
  • Munc18 Proteins / metabolism
  • Munc18 Proteins / physiology
  • Protein Binding
  • SNARE Proteins / metabolism*
  • SNARE Proteins / physiology*
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

Substances

  • Lipids
  • Membrane Proteins
  • Munc18 Proteins
  • SNARE Proteins
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins