Evidence map›Paper›PMID 32860428›Full record

ArticleFEBS letters2020

Arrangements of proteins at reconstituted synaptic vesicle fusion sites depend on membrane separation.

Lucy Ginger, Joerg Malsam, Andreas F-P Sonnen, Dustin Morado, Andrea Scheutzow, Thomas H Söllner, John A G Briggs

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Symmetrical arrangement of proteins under release-ready vesicles in presynaptic terminals.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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

7 authors at 3 institutions in 2 countries.

Lucy GingerMRC Laboratory of Molecular Biology, Cambridge, UK.
Joerg MalsamHeidelberg University Biochemistry Center, Heidelberg, Germany.
Andreas F-P SonnenStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Dustin MoradoMRC Laboratory of Molecular Biology, Cambridge, UK.
Andrea ScheutzowHeidelberg University Biochemistry Center, Heidelberg, Germany.
Thomas H SöllnerHeidelberg University Biochemistry Center, Heidelberg, Germany.
John A G BriggsMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID 0000-0003-3990-6910
Heidelberg University · DEMRC Laboratory of Molecular Biology · GBEuropean Molecular Biology Laboratory · DE

Funding

Medical Research Council MC_UP_1201/16
6 · The paper itself

Abstract

Synaptic vesicle proteins, including N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), Synaptotagmin-1 and Complexin, are responsible for controlling the synchronised fusion of synaptic vesicles with the presynaptic plasma membrane in response to elevated cytosolic calcium levels. A range of structures of SNAREs and their regulatory proteins have been elucidated, but the exact organisation of these proteins at synaptic junction membranes remains elusive. Here, we have used cryoelectron tomography to investigate the arrangement of synaptic proteins in an in vitro reconstituted fusion system. We found that the separation between vesicle and target membranes strongly correlates with the organisation of protein complexes at junctions. At larger membrane separations, protein complexes assume a 'clustered' distribution at the docking site, inducing a protrusion in the target membrane. As the membrane separation decreases, protein complexes become displaced radially outwards and assume a 'ring-like' arrangement. Our findings indicate that docked vesicles can possess a wide range of protein complex numbers and be heterogeneous in their protein arrangements.

Indexed as

Cell MembraneCryoelectron MicroscopyIn Vitro TechniquesMembrane ProteinsSynaptic VesiclesTomographyMembrane Proteinscryoelectron tomographyfusionin vitro reconstitutionmembraneSNAREsynaptic vesicle

Identifiers

PMID32860428
PMCPMC7711843
OpenAlexW3081700655

What OpenQuestion holds

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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.