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Role of the synaptobrevin C terminus in fusion pore formation.

Authors
  • Ngatchou, Annita N
  • Kisler, Kassandra
  • Fang, Qinghua
  • Walter, Alexander M
  • Zhao, Ying
  • Bruns, Dieter
  • Sørensen, Jakob B
  • Lindau, Manfred
Type
Published Article
Journal
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Publication Date
Oct 26, 2010
Volume
107
Issue
43
Pages
18463–18468
Identifiers
DOI: 10.1073/pnas.1006727107
PMID: 20937897
Source
Medline
License
Unknown

Abstract

Neurotransmitter release is mediated by the SNARE proteins synaptobrevin II (sybII, also known as VAMP2), syntaxin, and SNAP-25, generating a force transfer to the membranes and inducing fusion pore formation. However, the molecular mechanism by which this force leads to opening of a fusion pore remains elusive. Here we show that the ability of sybII to support exocytosis is inhibited by addition of one or two residues to the sybII C terminus depending on their energy of transfer from water to the membrane interface, following a Boltzmann distribution. These results suggest that following stimulation, the SNARE complex pulls the C terminus of sybII deeper into the vesicle membrane. We propose that this movement disrupts the vesicular membrane continuity leading to fusion pore formation. In contrast to current models, the experiments suggest that fusion pore formation begins with molecular rearrangements at the intravesicular membrane leaflet and not between the apposed cytoplasmic leaflets.

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