Specificity and regulation of a synaptic vesicle docking complex

Jonathan Pevsner, Shu Chan Hsu, Janice E.A. Braun, Nicole Calakos, Anthony E. Ting, Mark K. Bennett, Richard H. Scheller

Research output: Contribution to journalArticlepeer-review

510 Scopus citations


Synaptic vesicles are proposed to dock at the presynaptic plasma membrane through the interaction of two integral membrane proteins of synaptic vesicles, VAMP and synaptotagmin, and two plasma membrane proteins, syntaxin and SNAP-25. We have characterized the binding properties of these proteins and observed SNAP-25 potentiation of VAMP 2 binding to syntaxins la and 4 but not syntaxins 2 or 3. n-sec1, a neuron-specific syntaxin-binding protein, bound syntaxin with nanomolar affinity, forming a complex that is distinct from the previously identified 7S and 20S syntaxin-containing complexes. This suggests that syntaxin exists in at least three states: bound to n-sec1, in a 7S particle, and in a 20S particle. Recombinant n-secl inhibited VAMP or SNAP-25 binding to syntaxin. We propose that the specific associations of VAMP, SNAP-25, and syntaxin mediate vesicle docking and that a syntaxin/n-sec1 complex precedes and/or regulates formation of these complexes.

Original languageEnglish (US)
Pages (from-to)353-361
Number of pages9
Issue number2
StatePublished - Aug 1994
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)


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