Evidence map›Paper›PMID 28621666›Full record

ArticleeLife2017

9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.

Svetlana O Dodonova, Patrick Aderhold, Juergen Kopp, Iva Ganeva, Simone Röhling, Wim J H Hagen, Irmgard Sinning, Felix Wieland, John A G Briggs

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

68 citing papers in PubMed, 121 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. A class of COPI cargo receptors regulates processing of transmembrane proteins by reinforcing their Golgi retention.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. bioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. Structural elucidation of how ARF small GTPases induce membrane tubulation for vesicle fission.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

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

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.

Svetlana O DodonovaStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0002-5002-8138
Patrick AderholdHeidelberg University Biochemistry Center, Heidelberg University, Heidelberg, Germany.
Juergen KoppHeidelberg University Biochemistry Center, Heidelberg University, Heidelberg, Germany.
Iva GanevaHeidelberg University Biochemistry Center, Heidelberg University, Heidelberg, Germany.
Simone RöhlingHeidelberg University Biochemistry Center, Heidelberg University, Heidelberg, Germany.
Wim J H HagenStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0001-6229-2692
Irmgard SinningHeidelberg University Biochemistry Center, Heidelberg University, Heidelberg, Germany.
Felix WielandHeidelberg University Biochemistry Center, Heidelberg University, Heidelberg, Germany.
John A G BriggsStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0003-3990-6910
Heidelberg University · DEEuropean Molecular Biology Laboratory · DEMax Planck Institute for Biophysical Chemistry · DEMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_UP_1201/16
6 · The paper itself

Abstract

COPI coated vesicles mediate trafficking within the Golgi apparatus and between the Golgi and the endoplasmic reticulum. Assembly of a COPI coated vesicle is initiated by the small GTPase Arf1 that recruits the coatomer complex to the membrane, triggering polymerization and budding. The vesicle uncoats before fusion with a target membrane. Coat components are structurally conserved between COPI and clathrin/adaptor proteins. Using cryo-electron tomography and subtomogram averaging, we determined the structure of the COPI coat assembled on membranes in vitro at 9 Å resolution. We also obtained a 2.57 Å resolution crystal structure of βδ-COP. By combining these structures we built a molecular model of the coat. We additionally determined the coat structure in the presence of ArfGAP proteins that regulate coat dissociation. We found that Arf1 occupies contrasting molecular environments within the coat, leading us to hypothesize that some Arf1 molecules may regulate vesicle assembly while others regulate coat disassembly.

Indexed as

ADP-Ribosylation Factor 1AnimalsCoat Protein Complex ICryoelectron MicroscopyCrystallography, X-RayElectron Microscope TomographyGTP PhosphohydrolasesMiceModels, MolecularProtein ConformationADP-Ribosylation Factor 1Coat Protein Complex IGTP PhosphohydrolasesArf1ArfGAPbiophysicscell biologycoated vesiclesCOPI coatcryo-electron tomographynonestructural biologysubtomogram averaging

Identifiers

PMID28621666
PMCPMC5482573
OpenAlexW2626951342

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.