Evidence map›Paper›PMID 26578768›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural basis for the binding of tryptophan-based motifs by δ-COP.

Richard J Suckling, Pak Phi Poon, Sophie M Travis, Irina V Majoul, Frederick M Hughson, Philip R Evans, Rainer Duden, David J Owen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.2field-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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. 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
  3. Article
  4. Article
  5. Article
  6. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Review
  17. Review
  18. Recycling of Golgi glycosyltransferases requires direct binding to coatomer.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Protein sorting at the ER-Golgi interface.The Journal of cell biology · 2016
    Review
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 6 institutions in 4 countries.

Richard J SucklingMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom; Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom;
Pak Phi PoonDepartment of Microbiology and Immunology, Dalhousie University, Halifax, N.S., Canada B3H 4R2;
Sophie M TravisDepartment of Molecular Biology, Princeton University, Princeton NJ 08544;
Irina V MajoulInstitute of Biology, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23562 Lübeck, Germany.
Frederick M HughsonDepartment of Molecular Biology, Princeton University, Princeton NJ 08544;
Philip R EvansMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom;
Rainer DudenInstitute of Biology, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23562 Lübeck, Germany duden@bio.uni-luebeck.de djo30@cam.ac.uk.
David J OwenCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom; duden@bio.uni-luebeck.de djo30@cam.ac.uk.
Princeton University · USUniversity of Lübeck · DEDalhousie University · CAMedical Research Council · GBMRC Laboratory of Molecular Biology · GBUniversity of Cambridge · GB

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Structural Analysis of Membrane Tethering and Fusion ProteinsR01GM071574 · NIGMS · PRINCETON UNIVERSITY · PI HUGHSON, FREDERICK M · 2005 to 2024
$6.8M
CIHRMedical Research Council MC_U105178845Medical Research Council U105178845NIGMS NIH HHS GM071574NIGMS NIH HHS R01 GM071574NIGMS NIH HHS T32 GM007388Wellcome Trust 090909Wellcome Trust 100140
6 · The paper itself

Abstract

Coatomer consists of two subcomplexes: the membrane-targeting, ADP ribosylation factor 1 (Arf1):GTP-binding βγδζ-COP F-subcomplex, which is related to the adaptor protein (AP) clathrin adaptors, and the cargo-binding αβ'ε-COP B-subcomplex. We present the structure of the C-terminal μ-homology domain of the yeast δ-COP subunit in complex with the WxW motif from its binding partner, the endoplasmic reticulum-localized Dsl1 tether. The motif binds at a site distinct from that used by the homologous AP μ subunits to bind YxxΦ cargo motifs with its two tryptophan residues sitting in compatible pockets. We also show that the Saccharomyces cerevisiae Arf GTPase-activating protein (GAP) homolog Gcs1p uses a related WxxF motif at its extreme C terminus to bind to δ-COP at the same site in the same way. Mutations designed on the basis of the structure in conjunction with isothermal titration calorimetry confirm the mode of binding and show that mammalian δ-COP binds related tryptophan-based motifs such as that from ArfGAP1 in a similar manner. We conclude that δ-COP subunits bind Wxn(1-6)[WF] motifs within unstructured regions of proteins that influence the lifecycle of COPI-coated vesicles; this conclusion is supported by the observation that, in the context of a sensitizing domain deletion in Dsl1p, mutating the tryptophan-based motif-binding site in yeast causes defects in both growth and carboxypeptidase Y trafficking/processing.

Indexed as

Amino Acid MotifsCalorimetry, IndirectCathepsin ACoatomer ProteinCOP-Coated VesiclesDNA-Binding ProteinsGTPase-Activating ProteinsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTryptophanCathepsin ACoatomer ProteinDNA-Binding ProteinsDSL1 protein, S cerevisiaeGCS1 protein, S cerevisiaeGTPase-Activating ProteinsPRC1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTryptophancoatomerCOPImembrane traffickingvesicle coatδ-COP μ homology domain-binding motifs

Identifiers

PMID26578768
PMCPMC4655537
OpenAlexW2216922721

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.