Evidence map›Paper›PMID 33558502›Full record

ArticleNature communications2021

Cross-linking mass spectrometry uncovers protein interactions and functional assemblies in synaptic vesicle membranes.

Sabine Wittig, Marcelo Ganzella, Marie Barth, Susann Kostmann, Dietmar Riedel, Ángel Pérez-Lara, Reinhard Jahn, Carla Schmidt

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
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  6. Progress toward a comprehensive brain protein interactome.Biochemical Society transactions · 2025
    Review
  7. Review
  8. Molecular architecture of synaptic vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Phospholipids Differentially Regulate CaACS chemical biology · 2024
    Article
  12. Article
  13. Review
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  15. Article
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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

8 authors at 3 institutions in 2 countries.

Sabine WittigInterdisciplinary Research Centre HALOmem, Charles Tanford Protein Centre, Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle, Germany.
Marcelo GanzellaDepartment for Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Marie BarthInterdisciplinary Research Centre HALOmem, Charles Tanford Protein Centre, Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle, Germany.ORCID 0000-0001-5006-9573
Susann KostmannInterdisciplinary Research Centre HALOmem, Charles Tanford Protein Centre, Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle, Germany.
Dietmar RiedelDepartment for Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0003-2970-6894
Ángel Pérez-LaraDepartment for Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.ORCID 0000-0002-2736-3501
Reinhard JahnDepartment for Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Carla SchmidtInterdisciplinary Research Centre HALOmem, Charles Tanford Protein Centre, Institute for Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle, Germany. carla.schmidt@biochemtech.uni-halle.de.ORCID 0000-0001-9410-1424
Martin Luther University Halle-Wittenberg · DEMax Planck Institute for Biophysical Chemistry · DEUniversidad de Granada · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptic vesicles are storage organelles for neurotransmitters. They pass through a trafficking cycle and fuse with the pre-synaptic membrane when an action potential arrives at the nerve terminal. While molecular components and biophysical parameters of synaptic vesicles have been determined, our knowledge on the protein interactions in their membranes is limited. Here, we apply cross-linking mass spectrometry to study interactions of synaptic vesicle proteins in an unbiased approach without the need for specific antibodies or detergent-solubilisation. Our large-scale analysis delivers a protein network of vesicle sub-populations and functional assemblies including an active and an inactive conformation of the vesicular ATPase complex as well as non-conventional arrangements of the luminal loops of SV2A, Synaptophysin and structurally related proteins. Based on this network, we specifically target Synaptobrevin-2, which connects with many proteins, in different approaches. Our results allow distinction of interactions caused by 'crowding' in the vesicle membrane from stable interaction modules.

Indexed as

Mass SpectrometryAnimalsBrainCross-Linking ReagentsMembrane FusionProtein BindingProtein Interaction MapsProteolipidsProteomeRatsSynaptic MembranesSynaptic VesiclesSynaptophysinVacuolar Proton-Translocating ATPasesVesicle-Associated Membrane Protein 2Cross-Linking ReagentsProteolipidsproteoliposomesProteomeSynaptophysinVacuolar Proton-Translocating ATPasesVesicle-Associated Membrane Protein 2

Identifiers

PMID33558502
PMCPMC7870876
OpenAlexW3128476683

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.