Complexin induces a conformational change at the membrane-proximal C-terminal end of the SNARE complex

Elife. 2016 Jun 2:5:e16886. doi: 10.7554/eLife.16886.

Abstract

Complexin regulates spontaneous and activates Ca(2+)-triggered neurotransmitter release, yet the molecular mechanisms are still unclear. Here we performed single molecule fluorescence resonance energy transfer experiments and uncovered two conformations of complexin-1 bound to the ternary SNARE complex. In the cis conformation, complexin-1 induces a conformational change at the membrane-proximal C-terminal end of the ternary SNARE complex that specifically depends on the N-terminal, accessory, and central domains of complexin-1. The complexin-1 induced conformation of the ternary SNARE complex may be related to a conformation that is juxtaposing the synaptic vesicle and plasma membranes. In the trans conformation, complexin-1 can simultaneously interact with a ternary SNARE complex via the central domain and a binary SNARE complex consisting of syntaxin-1A and SNAP-25A via the accessory domain. The cis conformation may be involved in activation of synchronous neurotransmitter release, whereas both conformations may be involved in regulating spontaneous release.

Keywords: biophysics; calcium triggering; neuroscience; neurotransmitter release; rat; structural biology; synaptic vesicle fusion.

Publication types

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

MeSH terms

  • Adaptor Proteins, Vesicular Transport / chemistry
  • Adaptor Proteins, Vesicular Transport / metabolism
  • Animals
  • Cell Membrane / metabolism
  • Fluorescence Resonance Energy Transfer / methods
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • Protein Binding
  • Protein Conformation
  • Rats
  • SNARE Proteins / chemistry*
  • SNARE Proteins / metabolism
  • Synaptosomal-Associated Protein 25 / chemistry
  • Synaptosomal-Associated Protein 25 / metabolism
  • Syntaxin 1 / chemistry
  • Syntaxin 1 / metabolism

Substances

  • Adaptor Proteins, Vesicular Transport
  • Nerve Tissue Proteins
  • SNARE Proteins
  • Synaptosomal-Associated Protein 25
  • Syntaxin 1
  • complexin I