ArticleThe Journal of membrane biology2010
SNARE complex zipping as a driving force in the dilation of proteinaceous fusion pores.
Article in The Journal of membrane biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 43 citations in OpenAlex.
- Membrane Merger Dynamics in Exocytosis and Endocytosis.Advances in experimental medicine and biology · 2026Review
- Using multiscale molecular dynamics simulations to explore the fusion machinery underlying neurotransmitter release.Quarterly reviews of biophysics · 2025Review
- SNARE complex assembly and disassembly dynamics in response to CaBiophysical journal · 2025Article
- Exploring the structural dynamics of the vesicle priming machinery.Biochemical Society transactions · 2024Review
- Differential SNARE chaperoning by Munc13-1 and Munc18-1 dictates fusion pore fate at the release site.Nature communications · 2024Article
- All SNAP25 molecules in the vesicle-plasma membrane contact zone change conformation during vesicle priming.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Double-Transmembrane Domain of SNAREs Decelerates the Fusion by Increasing the Protein-Lipid Mismatch.Journal of molecular biology · 2023Article
- Illuminating membrane structural dynamics of fusion and endocytosis with advanced light imaging techniques.Biochemical Society transactions · 2022Review
- Stability profile of the neuronal SNARE complex reflects its potency to drive fast membrane fusion.Biophysical journal · 2022Article
- Hypothesis Relating the Structure, Biochemistry and Function of Active Zone Material Macromolecules at a Neuromuscular Junction.Frontiers in synaptic neuroscience · 2021Article
- Synaptic Vesicles Having Large Contact Areas with the Presynaptic Membrane are Preferentially Hemifused at Active Zones of Frog Neuromuscular Junctions Fixed during Synaptic Activity.International journal of molecular sciences · 2019Review
- 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
- Syntaxins on granules promote docking of granules via interactions with munc18.Scientific reports · 2018Article
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- Article
- Fusion pores and their control of neurotransmitter and hormone release.The Journal of general physiology · 2017Review
- The Structure of the Synaptic Vesicle-Plasma Membrane Interface Constrains SNARE Models of Rapid, Synchronous Exocytosis at Nerve Terminals.Frontiers in molecular neuroscience · 2017Review
- Article
- Lipid-anchored Synaptobrevin Provides Little or No Support for Exocytosis or Liposome Fusion.The Journal of biological chemistry · 2016Article
- The Hydrophobic Effect in Solute Partitioning and Interfacial Tension.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The assembly of SNARE proteins into a tight complex has been hypothesized to drive membrane fusion. A model of the initial fusion pore as a proteinaceous channel formed by SNARE proteins places their membrane anchors in separate membranes. This leaves the possibility of a final assembly step that brings the membrane anchors together and drives fusion pore expansion. The present study develops a model for expansion in which the final SNARE complex zipping step drives a transition from a proteinaceous fusion pore to a lipidic fusion pore. An estimate of the energy released upon merger of the helical segments of the SNARE motifs with the helical segments of the membrane anchors indicates that completing the assembly of a few SNARE complexes can overcome the elastic energy that opposes lipid bilayer deformation into a narrow fusion pore. The angle between the helical axes of the membrane anchor and SNARE motif serves as a useful reaction coordinate for this transition. Energy was calculated as a function of this angle, incorporating contributions from membrane bending, SNARE complex assembly, membrane anchor flexing and hydrophobic interactions. The rate of this transition was evaluated as a process of diffusion over the barrier imposed by these combined energies, and the rates estimated were consistent with experimental measurements.
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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.