Evidence map›Paper›PMID 17954604›Full record

ArticleThe Journal of cell biology2007

Novel cargo-binding site in the beta and delta subunits of coatomer.

Kai Michelsen, Volker Schmid, Jutta Metz, Katja Heusser, Urban Liebel, Torsten Schwede, Anne Spang, Blanche Schwappach

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 68 citations in OpenAlex.

  1. Amyloid-β "Co-assembles" with Coatomer Subunit Delta (δ-COP).The journal of physical chemistry letters · 2026
    Article
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  5. Subcellular trafficking and endocytic recycling of KAmerican journal of physiology. Cell physiology · 2022
    Review
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  11. Review
  12. Protein sorting at the ER-Golgi interface.The Journal of cell biology · 2016
    Review
  13. δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
  15. Article
  16. Review
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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

8 authors at 4 institutions in 2 countries.

Kai MichelsenZentrum für Molekulare Biologie der Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany.
Volker Schmid
Jutta Metz
Katja Heusser
Urban Liebel
Torsten Schwede
Anne Spang
Blanche Schwappach
Heidelberg University · DEEuropean Molecular Biology Laboratory · DESIB Swiss Institute of Bioinformatics · CHUniversity of Basel · CH

Funding

Wellcome Trust 081671
6 · The paper itself

Abstract

Arginine (R)-based ER localization signals are sorting motifs that confer transient ER localization to unassembled subunits of multimeric membrane proteins. The COPI vesicle coat binds R-based signals but the molecular details remain unknown. Here, we use reporter membrane proteins based on the proteolipid Pmp2 fused to GFP and allele swapping of COPI subunits to map the recognition site for R-based signals. We show that two highly conserved stretches--in the beta- and delta-COPI subunits--are required to maintain Pmp2GFP reporters exposing R-based signals in the ER. Combining a deletion of 21 residues in delta-COP together with the mutation of three residues in beta-COP gave rise to a COPI coat that had lost its ability to recognize R-based signals, whilst the recognition of C-terminal di-lysine signals remained unimpaired. A homology model of the COPI trunk domain illustrates the recognition of R-based signals by COPI.

Indexed as

Adaptor Protein Complex 1Amino Acid SequenceArginineBinding SitesCoatomer ProteinConserved SequenceEndoplasmic ReticulumGenes, FungalMolecular Sequence DataMutant ProteinsMutationProtein Sorting SignalsProtein SubunitsProtein TransportSaccharomyces cerevisiaeStructural Homology, ProteinAdaptor Protein Complex 1ArginineCoatomer ProteinMutant ProteinsProtein Sorting SignalsProtein Subunits

Identifiers

PMID17954604
PMCPMC2064757
OpenAlexW2052496852

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.