Evidence map›Paper›PMID 7835333›Full record

ArticleThe EMBO journal1995

Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine.

L Edelmann, P I Hanson, E R Chapman, R Jahn

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.

0numbers the graph read from it
0cells of the map it votes in
127citing papers in PubMed
15.4field-weighted citation impact, top 1% 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

127 citing papers in PubMed, 455 citations in OpenAlex.

  1. Synaptobrevin-2 disease variants reveal spatial constraints within the presynaptic active zone.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  5. Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  10. Review
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  14. The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core Vesicle Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  15. Article
  16. Room for Two: The Synaptophysin/Synaptobrevin Complex.Frontiers in synaptic neuroscience · 2021
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  17. Review
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  20. Article

67 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 2 institutions in 1 country.

L EdelmannHoward Hughes Medical Institute, Yale University School of Medicine, New Haven CT 06510.
P I Hanson
E R Chapman
R Jahn
Yale University · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synaptic vesicle protein synaptobrevin (VAMP) has recently been implicated as one of the key proteins involved in exocytotic membrane fusion. It interacts with the synaptic membrane proteins syntaxin I and synaptosome-associated protein (SNAP)-25 to form a complex which precedes exocytosis [Söllner et al. (1993b) Cell, 75, 409-418]. Here we demonstrate that the majority of synaptobrevin is bound to the vesicle protein synaptophysin in detergent extracts. No syntaxin I was found in this complex when synaptophysin-specific antibodies were used for immunoprecipitation. Conversely, no synaptophysin was associated with the synaptobrevin-syntaxin I complex when syntaxin-specific antibodies were used for immunoprecipitation. Thus, the synaptobrevin pool bound to synaptophysin is not available for binding to syntaxin I and SNAP-25, and vice versa. Synaptobrevin-synaptophysin binding was also demonstrated by chemical cross-linking in isolated nerve terminals. Furthermore, recombinant synaptobrevin II efficiently bound synaptophysin and its isoform synaptoporin, but not the more distantly related synaptic vesicle protein p29. Recombinant synaptobrevin I bound with similar efficiency, whereas the non-neuronal isoform cellubrevin displayed a lower affinity towards synaptophysin. Treatment with high NaCl concentrations resulted in a dissociation of the synaptobrevin-synaptophysin complex. In addition, the interaction of synaptobrevin with synaptophysin was irreversibly abolished by low amounts of SDS, while the interaction with syntaxin I was enhanced. We conclude that synaptophysin selectively interacts with synaptobrevin in a complex which excludes the t-SNAP receptors syntaxin I and SNAP-25, suggesting a role for synaptophysin in the control of exocytosis.

Indexed as

Cell FusionExocytosisAmino Acid SequenceAnimalsCross-Linking ReagentsMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsPrecipitin TestsProtein BindingRatsR-SNARE ProteinsSynaptophysinCross-Linking ReagentsMembrane ProteinsNerve Tissue ProteinsR-SNARE ProteinsSynaptophysin

Identifiers

PMID7835333
PMCPMC398074
OpenAlexW185955435

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.