ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2015
A structural role for the synaptobrevin 2 transmembrane domain in dense-core vesicle fusion pores.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 53 citations in OpenAlex.
- Synaptobrevin-2 Containing Extracellular Vesicles Are Rapidly Incorporated Into Mammalian Neurons via a Dynamin-Dependent Pathway.Journal of neurochemistry · 2026Article
- Membrane Merger Dynamics in Exocytosis and Endocytosis.Advances in experimental medicine and biology · 2026Review
- Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Synaptobrevin2 monomers and dimers differentially engage to regulate the functional trans-SNARE assembly.Life science alliance · 2024Article
- Article
- Membrane transformations of fusion and budding.Nature communications · 2024Review
- Three membrane fusion pore families determine the pathway to pore dilation.Biophysical journal · 2023Article
- Synaptophysin transmembrane domain III controls fusion pore dynamics in CaBiophysical journal · 2023Article
- Designer Nanodiscs to Probe and Reprogram Membrane Biology in Synapses.Journal of molecular biology · 2023Review
- Illuminating membrane structural dynamics of fusion and endocytosis with advanced light imaging techniques.Biochemical Society transactions · 2022Review
- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- Smuggle tau through a secret(ory) pathway.The Biochemical journal · 2021Article
- Recordings from neuron-HEK cell cocultures reveal the determinants of miniature excitatory postsynaptic currents.The Journal of general physiology · 2021Article
- The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core Vesicle Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Fusion Pore Expansion and Contraction during Catecholamine Release from Endocrine Cells.Biophysical journal · 2020Article
- Tetanus insensitive VAMP2 differentially restores synaptic and dense core vesicle fusion in tetanus neurotoxin treated neurons.Scientific reports · 2020Article
- Carbon-Fiber Nanoelectrodes for Real-Time Discrimination of Vesicle Cargo in the Native Cellular Environment.ACS nano · 2020Article
- 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
- Synaptobrevin-2 C-Terminal Flexible Region Regulates the Discharge of Catecholamine Molecules.Biophysical journal · 2019Article
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6 authors at 4 institutions in 2 countries.
Funding
Abstract
Ca(2+)-triggered release of neurotransmitters and hormones depends on soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) to drive the fusion of the vesicle and plasma membranes. The formation of the SNARE complex by the vesicle SNARE synaptobrevin 2 (syb2) and the two plasma membrane SNAREs syntaxin (syx) and SNAP-25 draws the two membranes together, but the events that follow membrane juxtaposition, and the ways that SNAREs remodel lipid membranes remain poorly understood. The SNAREs syx and syb2 have transmembrane domains (TMDs) that can exert force directly on the lipid bilayers. The TMD of syx influences fusion pore flux in a manner that suggests it lines the nascent fusion pore through the plasma membrane. The TMD of syb2 traverses the vesicle membrane and is the most likely partner to syx in completing a proteinaceous fusion pore through the vesicle membrane, but the role of this vesicle SNARE in fusion pores has yet to be tested. Here amperometry and conductance measurements were performed to probe the function of the syb2 TMD in fusion pores formed during catecholamine exocytosis in mouse chromaffin cells. Fusion pore flux was sensitive to the size and charge of TMD residues near the N terminus; fusion pore conductance was altered by substitutions at these sites. Unlike syx, the syb2 residues that influence fusion pore permeation fell along two α-helical faces of its TMD, rather than one. These results indicate a role for the syb2 TMD in nascent fusion pores, but in a very different structural arrangement from that of the syx TMD.
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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.