Evidence map›Paper›PMID 22174414›Full record

ArticleThe Journal of biological chemistry2012

Distinct contributions of vacuolar Qabc- and R-SNARE proteins to membrane fusion specificity.

Ryota Izawa, Toshitaka Onoue, Noriko Furukawa, Joji Mima

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. A look beyond the QR code of SNARE proteins.Protein science : a publication of the Protein Society · 2024
    Article
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  7. Article
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  9. Article
  10. Homotypic and heterotypicThe Journal of biological chemistry · 2019
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. CAPS and Munc13: CATCHRs that SNARE Vesicles.Frontiers in endocrinology · 2013
    Review
  20. 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

4 authors at 2 institutions in 1 country.

Ryota IzawaInstitute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.
Toshitaka Onoue
Noriko Furukawa
Joji Mima
Osaka University · JPProtein Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotic endomembrane systems, Qabc-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) on one membrane and R-SNARE on the opposing membrane assemble into a trans-QabcR-SNARE complex to drive membrane fusion. However, it remains ambiguous whether pairing of Qabc- and R-SNAREs mediates membrane fusion specificity. Here, we explored the fusion specificity of reconstituted proteoliposomes bearing purified SNAREs in yeast vacuoles and other organelles. We found that not only vacuolar R-SNARE Nyv1p but also the non-cognate R-SNAREs, endosomal Snc2p, and endoplasmic reticulum-Golgi Sec22p caused efficient fusion with vacuolar Qabc-SNAREs. In contrast, their fusion is blocked completely by replacing vacuolar Qc-SNARE Vam7p with the non-cognate endosomal Tlg1p and Syn8p, although these endosomal Qc-SNAREs fully retained the ability to form cis-SNARE complexes with vacuolar SNAREs in solution and on membranes. Thus, our current study establishes that an appropriate assembly of Qabc-SNAREs is crucial for regulating fusion specificity, whereas R-SNARE itself has little contribution to specificity.

Indexed as

Endoplasmic ReticulumEndosomesIntracellular MembranesMembrane FusionMembrane ProteinsR-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSynaptosomal-Associated Protein 25Membrane ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSynaptosomal-Associated Protein 25Tlg1 protein, S cerevisiaeVAM7 protein, S cerevisiae

Identifiers

PMID22174414
PMCPMC3270998
OpenAlexW2002774460

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.