Evidence map›Paper›PMID 19458617›Full record

ArticleNature2009

Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes.

Takeshi Ohya, Marta Miaczynska, Unal Coskun, Barbara Lommer, Anja Runge, David Drechsel, Yannis Kalaidzidis, Marino Zerial

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 127 papers.

0numbers the graph read from it
0cells of the map it votes in
127citing papers in PubMed
10.8field-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, 234 citations in OpenAlex.

  1. The Rab5 effector Rabankyrin-5 mediates endosomal fusion and trafficking of human papillomavirus during early entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. ELAPOR1 is a copper-dependent tethering factor driving proacrosomal vesicle fusion during acrosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Synthetic Lipid Biology.Chemical reviews · 2025
    Review
  4. Article
  5. Function and regulation of Rab GTPases in cancers.Cell biology and toxicology · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Frontiers in microbiology · 2023
    Article
  12. Review
  13. Article
  14. Article
  15. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 2 countries.

Takeshi OhyaMax Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany.
Marta Miaczynska
Unal Coskun
Barbara Lommer
Anja Runge
David Drechsel
Yannis Kalaidzidis
Marino Zerial
Max Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rab GTPases and SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) are evolutionarily conserved essential components of the eukaryotic intracellular transport system. Although pairing of cognate SNAREs is sufficient to fuse membranes in vitro, a complete reconstitution of the Rab-SNARE machinery has never been achieved. Here we report the reconstitution of the early endosomal canine Rab5 GTPase, its key regulators and effectors together with SNAREs into proteoliposomes using a set of 17 recombinant human proteins. These vesicles behave like minimal 'synthetic' endosomes, fusing with purified early endosomes or with each other in vitro. Membrane fusion measured by content-mixing and morphological assays requires the cooperativity between Rab5 effectors and cognate SNAREs which, together, form a more efficient 'core machinery' than SNAREs alone. In reconstituting a fusion mechanism dependent on both a Rab GTPase and SNAREs, our work shows that the two machineries act coordinately to increase the specificity and efficiency of the membrane tethering and fusion process.

Indexed as

AnimalsCell LineCricetinaeCytosolDogsEndosomesHumansMembrane FusionMicroscopy, ElectronProteolipidsrab GTP-Binding ProteinsRecombinant ProteinsSNARE ProteinsVesicular Transport ProteinsProteolipidsproteoliposomesrab GTP-Binding ProteinsRecombinant ProteinsSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID19458617
OpenAlexW1978391620

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.