ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012
Membrane-proximal tryptophans of synaptobrevin II stabilize priming of secretory vesicles.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- From Membrane Composition to Antimicrobial Strategies: Experimental and Computational Approaches to AMP Design and Selectivity.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- Article
- Structural Roles for the Juxtamembrane Linker Region and Transmembrane Region of Synaptobrevin 2 in Membrane Fusion.Frontiers in cell and developmental biology · 2020Article
- Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE.Cell reports · 2019Article
- Retrograde trafficking and quality control of yeast synaptobrevin, Snc1, are conferred by its transmembrane domain.Molecular biology of the cell · 2019Article
- Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly.Nature communications · 2019Article
- Article
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017Review
- Fusion pores and their control of neurotransmitter and hormone release.The Journal of general physiology · 2017Review
- The Multifaceted Role of SNARE Proteins in Membrane Fusion.Frontiers in physiology · 2017Review
- The Molecular Switching Mechanism at the Conserved D(E)RY Motif in Class-A GPCRs.Biophysical journal · 2016Article
- Article
- Exploring the Formation and the Structure of Synaptobrevin Oligomers in a Model Membrane.Biophysical journal · 2016Article
- Lipid-anchored Synaptobrevin Provides Little or No Support for Exocytosis or Liposome Fusion.The Journal of biological chemistry · 2016Article
- Complexins: small but capable.Cellular and molecular life sciences : CMLS · 2015Review
- Synaptobrevin Transmembrane Domain Dimerization Studied by Multiscale Molecular Dynamics Simulations.Biophysical journal · 2015Article
- Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins.eLife · 2014Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trans-soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE) complexes formed between the SNARE motifs of synaptobrevin II, SNAP-25, and syntaxin play an essential role in Ca(2+)-regulated exocytosis. Apart from the well studied interactions of the SNARE domains, little is known about the functional relevance of other evolutionarily conserved structures in the SNARE proteins. Here, we show that substitution of two highly conserved tryptophan residues within the juxtamembrane domain (JMD) of the vesicular SNARE Synaptobrevin II (SybII) profoundly impairs priming of granules in mouse chromaffin cells without altering catecholamine release from single vesicles. Using molecular dynamic simulations of membrane-embedded SybII, we show that Trp residues of the JMD influence the electrostatic surface potential by controlling the position of neighboring lysine and arginine residues at the membrane-water interface. Our observations indicate a decisive role of the tryptophan moiety of SybII in keeping the vesicles in the release-ready state and support a model wherein tryptophan-mediated protein-lipid interactions assist in bridging the apposing membranes before fusion.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.