Evidence map›Paper›PMID 16339880›Full record

ArticleBiophysical journal2006

Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion.

S Moses Dennison, Mark E Bowen, Axel T Brunger, Barry R Lentz

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
5.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

78 citing papers in PubMed, 139 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartments.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. Homotypic and heterotypicThe Journal of biological chemistry · 2019
    Article
  10. Article
  11. Article
  12. Assembly of intermediates for rapid membrane fusion.The Journal of biological chemistry · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Towards reconstitution of membrane fusion mediated by SNAREs and other synaptic proteins.Critical reviews in biochemistry and molecular biology · 2015
    Review
  19. Article
  20. Review

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

S Moses DennisonDepartment of Biochemistry and Program in Molecular/Cell Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Mark E Bowen
Axel T Brunger
Barry R Lentz
University of North Carolina at Chapel Hill · USStanford Synchrotron Radiation Lightsource · USStanford University · US

Funding

STRUCTURE OF PROTEINS INVOLVED IN SYNAPTIC EXOCYTOSISR01MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2000 to 2025
$4.7M
Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
MICROSTRUCTURAL HETEROGENEITY IN MEMBRANESR01GM032707 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LENTZ, BARRY R · 1985 to 2010
$3.0M
NIGMS NIH HHS GM32707NIGMS NIH HHS R01 GM032707NIMH NIH HHS MH63105NIMH NIH HHS R01 MH063105NIMH NIH HHS R37 MH063105
6 · The paper itself

Abstract

At low surface concentrations that permit formation of impermeable membranes, neuronal soluble N-ethyl maleimide sensitive factor attachment protein receptor (SNARE) proteins form a stable, parallel, trans complex when vesicles are brought into contact by a low concentration of poly(ethylene glycol) (PEG). Surprisingly, formation of a stable SNARE complex does not trigger fusion under these conditions. However, neuronal SNAREs do promote fusion at low protein/lipid ratios when triggered by higher concentrations of PEG. Promotion of PEG-triggered fusion required phosphatidylserine and depended only on the surface concentration of SNAREs and not on the formation of a trans SNARE complex. These results were obtained at protein surface concentrations reported for synaptobrevin in synaptic vesicles and with an optimally fusogenic lipid composition. At a much higher protein/lipid ratio, vesicles joined by SNARE complex slowly mixed lipids at 37 degrees C in the absence of PEG, in agreement with earlier reports. However, vesicles containing syntaxin at a high protein/lipid ratio (>or=1:250) lost membrane integrity. We conclude that the neuronal SNARE complex promotes fusion by joining membranes and that the individual proteins syntaxin and synaptobrevin disrupt membranes so as to favor formation of a stalk complex and to promote conversion of the stalk to a fusion pore. These effects are similar to the effects of viral fusion peptides and transmembrane domains, but they are not sufficient by themselves to produce fusion in our in vitro system at surface concentrations documented to occur in synaptic vesicles. Thus, it is likely that proteins or factors other than the SNARE complex must trigger fusion in vivo.

Indexed as

Membrane FusionLiposomesMembrane Fusion ProteinsMembranes, ArtificialNerve Tissue ProteinsNeuronsPolyethylene GlycolsSNARE ProteinsSynaptic VesiclesLiposomesMembrane Fusion ProteinsMembranes, ArtificialNerve Tissue ProteinsPolyethylene GlycolsSNARE Proteins

Identifiers

PMID16339880
PMCPMC1367317
OpenAlexW2094866780

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.