Evidence map›Paper›PMID 20926670›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010

Quantitative analysis of synaptic vesicle Rabs uncovers distinct yet overlapping roles for Rab3a and Rab27b in Ca2+-triggered exocytosis.

Nathan J Pavlos, Mads Grønborg, Dietmar Riedel, John J E Chua, Janina Boyken, Tobias H Kloepper, Henning Urlaub, Silvio O Rizzoli, Reinhard Jahn

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

59 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Review
  3. The protein interactome of the Neuron Specific Gene family (NSG1-3).bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
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  6. Article
  7. Article
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  9. Review
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  11. p97/VCP Promotes the Recycling of Endocytic Cargo.Molecular biology of the cell · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. [Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2021
    Article
  20. Hidden proteome of synaptic vesicles in the mammalian brain.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

9 authors at 4 institutions in 2 countries.

Nathan J PavlosDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Mads Grønborg
Dietmar Riedel
John J E Chua
Janina Boyken
Tobias H Kloepper
Henning Urlaub
Silvio O Rizzoli
Reinhard Jahn
Max Planck Society · DEElectron (Ukraine) · UAEuropean Neuroscience Institute Göttingen · DEMax Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rab GTPases are molecular switches that orchestrate protein complexes before membrane fusion reactions. In synapses, Rab3 and Rab5 proteins have been implicated in the exo-endocytic cycling of synaptic vesicles (SVs), but an involvement of additional Rabs cannot be excluded. Here, combining high-resolution mass spectrometry and chemical labeling (iTRAQ) together with quantitative immunoblotting and fluorescence microscopy, we have determined the exocytotic (Rab3a, Rab3b, Rab3c, and Rab27b) and endocytic (Rab4b, Rab5a/b, Rab10, Rab11b, and Rab14) Rab machinery of SVs. Analysis of two closely related proteins, Rab3a and Rab27b, revealed colocalization in synaptic nerve terminals, where they reside on distinct but overlapping SV pools. Moreover, whereas Rab3a readily dissociates from SVs during Ca(2+)-triggered exocytosis, and is susceptible to membrane extraction by Rab-GDI, Rab27b persists on SV membranes upon stimulation and is resistant to GDI-coupled Rab retrieval. Finally, we demonstrate that selective modulation of the GTP/GDP switch mechanism of Rab27b impairs SV recycling, suggesting that Rab27b, probably in concert with Rab3s, is involved in SV exocytosis.

Indexed as

Genes, OverlappingAnimalsCalciumCalcium SignalingCells, CulturedExocytosisGuanosine DiphosphateGuanosine TriphosphateHippocampusPresynaptic TerminalsProteomerab3A GTP-Binding Proteinrab GTP-Binding ProteinsRatsSubcellular FractionsSynaptic VesiclesCalciumGuanosine DiphosphateGuanosine TriphosphateProteomeRab27b protein, ratrab3A GTP-Binding Proteinrab GTP-Binding Proteins

Identifiers

PMID20926670
PMCPMC6634719
OpenAlexW2064862804

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.