Nitric oxide modulates synaptic vesicle docking/fusion reactions

Mollie K. Meffert, Nicole C. Calakos, Richard H. Scheller, Howard Schulman

Research output: Contribution to journalArticle

Abstract

Nitric oxide (NO) stimulates calcium-independent neurotransmitter release from synaptosomes. NO-stimulated release was found to be inhibited by Botulinum neurotoxins that inactivate the core complex of synaptic proteins involved in the docking and fusion of synaptic vesicles. In experiments using recombinant proteins, NO donors increased formation of the VAMP/SNAP- 25/syntaxin 1a core complex and inhibited the binding of n-sec1 to syntaxin 1a. The combined effects of these activities is predicted to promote vesicle docking/fusion. The sulfhydryl reagent NEM inhibited the binding of n-sec1 to syntaxin 1a, while β-ME could reverse the NO-enhanced association of VAMP/SNAP-25/syntaxin 1a. These data suggest that post-translational modification of sulfhydryl groups by a nitrogen monoxide (likely to be NO+) alters the synaptic protein interactions that regulate neurotransmitter release and synaptic plasticity.

Original languageEnglish (US)
Pages (from-to)1229-1236
Number of pages8
JournalNeuron
Volume16
Issue number6
DOIs
StatePublished - Jun 1996
Externally publishedYes

ASJC Scopus subject areas

  • Neuroscience(all)

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