Single-molecule FRET study of SNARE-mediated membrane fusion

Biosci Rep. 2011 Dec;31(6):457-63. doi: 10.1042/BSR20110011.

Abstract

Membrane fusion is one of the most important cellular processes by which two initially distinct lipid bilayers merge their hydrophobic cores, resulting in one interconnected structure. Proteins, called SNARE (soluble N-ethylmaleimide-sensitive factor-attachment protein receptor), play a central role in the fusion process that is also regulated by several accessory proteins. In order to study the SNARE-mediated membrane fusion, the in vitro protein reconstitution assay involving ensemble FRET (fluorescence resonance energy transfer) has been used over a decade. In this mini-review, we describe several single-molecule-based FRET approaches that have been applied to this field to overcome the shortage of the bulk assay in terms of protein and fusion dynamics.

Publication types

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

MeSH terms

  • Fluorescence Resonance Energy Transfer / methods*
  • Kinetics
  • Lipid Bilayers / chemistry
  • Liposomes / chemistry
  • Liposomes / metabolism
  • Membrane Fusion / physiology*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology
  • Protein Binding
  • Protein Conformation
  • SNARE Proteins / chemistry*
  • SNARE Proteins / metabolism*
  • Vesicular Transport Proteins / chemistry
  • Vesicular Transport Proteins / metabolism*

Substances

  • Lipid Bilayers
  • Liposomes
  • Membrane Proteins
  • SNARE Proteins
  • Vesicular Transport Proteins