ArticleCellular and molecular neurobiology2012
SNAP-25 contains non-acylated thiol pairs that can form intrachain disulfide bonds: possible sites for redox modulation of neurotransmission.
Article in Cellular and molecular neurobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Multiple structural states in an intrinsically disordered protein, SNAP-25, using circular dichroism.Biophysical journal · 2025Article
- Reductive Reprogramming: A Not-So-Radical Hypothesis of Neurodegeneration Linking Redox Perturbations to Neuroinflammation and Excitotoxicity.Cellular and molecular neurobiology · 2019Review
- Intraviral interactome of Chikungunya virus reveals the homo-oligomerization and palmitoylation of structural protein TF.Biochemical and biophysical research communications · 2019Article
- Article
- The glutathione cycle shapes synaptic glutamate activity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Review
- Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.Biophysical journal · 2017Article
- Disulfide Stress Targets Modulators of Excitotoxicity in Otherwise Healthy Brains.Neurochemical research · 2016Article
- Assembly and Comparison of Plasma Membrane SNARE Acceptor Complexes.Biophysical journal · 2016Article
- Protein vicinal thiol oxidations in the healthy brain: not so radical links between physiological oxidative stress and neural cell activities.Neurochemical research · 2014Article
- Arsenic binding to proteins.Chemical reviews · 2013Review
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Intrachain disulfide bond formation among the cysteine thiols of SNAP-25, a component of the SNARE protein complex required for neurotransmitter release, has been hypothesized to link oxidative stress and inhibition of synaptic transmission. However, neither the availability in vivo of SNAP-25 thiols, which are known targets of S-palmitoylation, nor the tendency of these thiols to form intrachain disulfide bonds is known. We have examined, in rat brain extracts, both the availability of closely spaced, or vicinal, thiol pairs in SNAP-25 and the propensity of these dithiols toward disulfide bond formation using a method improved by us recently that exploits the high chemoselectivity of phenylarsine oxide (PAO) for vicinal thiols. The results show for the first time that a substantial fraction of soluble and, to a lesser extent, particulate SNAP-25 contain non-acylated PAO-binding thiol pairs and that these thiols in soluble SNAP-25 in particular have a high propensity toward disulfide bond formation. Indeed, disulfide bonds were detected in a small fraction of soluble SNAP-25 even under conditions designed to prevent or greatly limit protein thiol oxidation during experimental procedures. These results provide direct experimental support for the availability, in a subpopulation of SNAP-25, of vicinal thiols that may confer on one or more isoforms of this family of proteins a sensitivity to oxidative stress.
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