ArticleMolecular biology of the cell2007
Determinants of synaptobrevin regulation in membranes.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 70 citations in OpenAlex.
- Intermediate steps in the formation of neuronal SNARE complexes.The Journal of biological chemistry · 2024Article
- Tight docking of membranes before fusion represents a metastable state with unique properties.Nature communications · 2021Article
- SNARE Regulatory Proteins in Synaptic Vesicle Fusion and Recycling.Frontiers in molecular neuroscience · 2021Review
- Differential Diffusional Properties in Loose and Tight Docking Prior to Membrane Fusion.Biophysical journal · 2020Article
- Elevated synaptic vesicle release probability in synaptophysin/gyrin family quadruple knockouts.eLife · 2019Article
- A convenient protocol for generating giant unilamellar vesicles containing SNARE proteins using electroformation.Scientific reports · 2018Article
- Arrest ofThe Journal of biological chemistry · 2018Article
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- A Membrane-Fusion Model That Exploits a β-to-α Transition in the Hydrophobic Domains of Syntaxin 1A and Synaptobrevin 2.International journal of molecular sciences · 2017Article
- The Multifaceted Role of SNARE Proteins in Membrane Fusion.Frontiers in physiology · 2017Review
- Safeguards of Neurotransmission: Endocytic Adaptors as Regulators of Synaptic Vesicle Composition and Function.Frontiers in cellular neuroscience · 2017Review
- The iTRAPs: Guardians of Synaptic Vesicle Cargo Retrieval During Endocytosis.Frontiers in synaptic neuroscience · 2016Review
- A highly tilted membrane configuration for the prefusion state of synaptobrevin.Biophysical journal · 2014Article
- α-SNAP interferes with the zippering of the SNARE protein membrane fusion machinery.The Journal of biological chemistry · 2014Article
- Synaptic vesicle recycling: steps and principles.The EMBO journal · 2014Review
- The Sybtraps: control of synaptobrevin traffic by synaptophysin, α-synuclein and AP-180.Traffic (Copenhagen, Denmark) · 2014Review
- Membrane-proximal tryptophans of synaptobrevin II stabilize priming of secretory vesicles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Membrane fusion intermediates via directional and full assembly of the SNARE complex.Science (New York, N.Y.) · 2012Article
- Synaptotagmin-1 may be a distance regulator acting upstream of SNARE nucleation.Nature structural & molecular biology · 2011Article
- Docking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assay.Biophysical journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Neuronal exocytosis is driven by the formation of SNARE complexes between synaptobrevin 2 on synaptic vesicles and SNAP-25/syntaxin 1 on the plasma membrane. It has remained controversial, however, whether SNAREs are constitutively active or whether they are down-regulated until fusion is triggered. We now show that synaptobrevin in proteoliposomes as well as in purified synaptic vesicles is constitutively active. Potential regulators such as calmodulin or synaptophysin do not affect SNARE activity. Substitution or deletion of residues in the linker connecting the SNARE motif and transmembrane region did not alter the kinetics of SNARE complex assembly or of SNARE-mediated fusion of liposomes. Remarkably, deletion of C-terminal residues of the SNARE motif strongly reduced fusion activity, although the overall stability of the complexes was not affected. We conclude that although complete zippering of the SNARE complex is essential for membrane fusion, the structure of the adjacent linker domain is less critical, suggesting that complete SNARE complex assembly not only connects membranes but also drives fusion.
Indexed as
Identifiers
What OpenQuestion holds
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.