Evidence map›Paper›PMID 11970962›Full record

ArticleThe Journal of cell biology2002

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat.

Ulrike Rein, Uwe Andag, Rainer Duden, Hans Dieter Schmitt, Anne Spang

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.1field-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

51 citing papers in PubMed, 130 citations in OpenAlex.

  1. VAMP8 function reveals tight linkage between endocytic recycling and endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Membrane Fusion and SNAREs: Interaction with Ras Proteins.International journal of molecular sciences · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Functional characterization of 67 endocytic accessory proteins using multiparametric quantitative analysis of CCP dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Cross-Kingdom Activation ofJournal of bacteriology · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016
    Review
  19. Article
  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

5 authors at 3 institutions in 2 countries.

Ulrike ReinFriedrich Miescher Laboratory, Max Planck Society, D-72076 Tübingen, Germany.
Uwe Andag
Rainer Duden
Hans Dieter Schmitt
Anne Spang
Friedrich Miescher Laboratory · DEMax Planck Institute for Biophysical Chemistry · DEUniversity of Cambridge · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

In eukaryotic cells, secretion is achieved by vesicular transport. Fusion of such vesicles with the correct target compartment relies on SNARE proteins on both vesicle (v-SNARE) and the target membranes (t-SNARE). At present it is not clear how v-SNAREs are incorporated into transport vesicles. Here, we show that binding of ADP-ribosylation factor (ARF)-GTPase-activating protein (GAP) to ER-Golgi v-SNAREs is an essential step for recruitment of Arf1p and coatomer, proteins that together form the COPI coat. ARF-GAP acts catalytically to recruit COPI components. Inclusion of v-SNAREs into COPI vesicles could be mediated by direct interaction with the coat. The mechanisms by which v-SNAREs interact with COPI and COPII coat proteins seem to be different and may play a key role in determining specificity in vesicle budding.

Indexed as

Saccharomyces cerevisiae ProteinsVesicular Transport ProteinsADP-Ribosylation Factor 1ADP-Ribosylation FactorsCoat Protein Complex ICOP-Coated VesiclesDNA-Binding ProteinsEndoplasmic ReticulumFungal ProteinsGTPase-Activating ProteinsIntracellular MembranesMembrane ProteinsMicrosomesProtein BindingRecombinant Fusion ProteinsSNARE ProteinsADP-Ribosylation Factor 1ADP-Ribosylation FactorsCoat Protein Complex IDNA-Binding ProteinsFungal ProteinsGCS1 protein, S cerevisiaeGTPase-Activating ProteinsMembrane ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID11970962
PMCPMC2173288
OpenAlexW2112488154

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.