ArticleBiophysical journal2016
Exploring the Formation and the Structure of Synaptobrevin Oligomers in a Model Membrane.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Turbocharging synaptic transmission: 12 SNAREpins are required for rapid release of reconstituted synaptic vesicles.Science advances · 2026Article
- BCL-2 and BOK regulate apoptosis by interaction of their C-terminal transmembrane domains.EMBO reports · 2024Article
- Molecular phylogeny and missense mutations at envelope proteins across coronaviruses.Genomics · 2020Article
- Coarse Grained Molecular Dynamic Simulations for the Study of TNF Receptor Family Members' Transmembrane Organization.Frontiers in cell and developmental biology · 2020Article
- Oligomerisation of Synaptobrevin-2 Studied by Native Mass Spectrometry and Chemical Cross-Linking.Journal of the American Society for Mass Spectrometry · 2019Article
- The Transmembrane Domain of Synaptobrevin Influences Neurotransmitter Flux through Synaptic Fusion Pores.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Closely related, yet unique: Distinct homo- and heterodimerization patterns of G protein coupled chemokine receptors and their fine-tuning by cholesterol.PLoS computational biology · 2018Article
- Structural Model of the mIgM B-Cell Receptor Transmembrane Domain From Self-Association Molecular Dynamics Simulations.Frontiers in immunology · 2018Article
- The Multifaceted Role of SNARE Proteins in Membrane Fusion.Frontiers in physiology · 2017Review
- Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains.Frontiers in molecular neuroscience · 2017Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SNARE complexes have been shown to act cooperatively to enable the synaptic vesicle fusion in neuronal transmission at millisecond timescale. It has previously been suggested that the oligomerization of SNARE complexes required for cooperative action in fusion is mediated by interactions between transmembrane domains (TMDs). We study the oligomerization of synaptobrevin TMD using ensembles of molecular dynamics (MD) simulations at coarse-grained resolution for both the wild-type (WT) and selected mutants. Trimerization and tetramerization of the sybII WT and mutants displayed distinct kinetics depending both on the rate of dimerization and the availability of alternative binding interfaces. Interestingly, the tetramerization kinetics and propensity for the sybII W89A-W90A mutant was significantly increased as compared with the WT; the tryptophans in WT sybII impose sterical restraints on oligomer packing, thereby maintaining an appropriate plasticity and accessibility of sybII to the binding of its cognate SNARE partners during membrane fusion. Higher-order oligomeric models (ranging from pentamer to octamer), built by incremental addition of peptides to smaller oligomers, revealed substantial stability and high compactness. These larger sybII oligomers may induce membrane deformation, thereby possibly facilitating fast fusion exocytosis.
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