Evidence map›Paper›PMID 15504911›Full record

ArticleThe Journal of cell biology2004

The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi.

Alison K Gillingham, Amy Hin Yan Tong, Charles Boone, Sean Munro

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

50 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026
    Review
  4. Review
  5. Article
  6. Methods for Controlling Small GTPase Activity.Chembiochem : a European journal of chemical biology · 2025
    Review
  7. Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019
    Review
  14. The Physiological Functions of the Golgin Vesicle Tethering Proteins.Frontiers in cell and developmental biology · 2019
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  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

4 authors at 2 institutions in 2 countries.

Alison K GillinghamMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK.
Amy Hin Yan Tong
Charles Boone
Sean Munro
Medical Research Council · GBUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rud3p is a coiled-coil protein of the yeast cis-Golgi. We find that Rud3p is localized to the Golgi via a COOH-terminal domain that is distantly related to the GRIP domain that recruits several coiled-coil proteins to the trans-Golgi by binding the small Arf-like GTPase Arl1p. In contrast, Rud3p binds to the GTPase Arf1p via this COOH-terminal "GRIP-related Arf-binding" (GRAB) domain. Deletion of RUD3 is lethal in the absence of the Golgi GTPase Ypt6p, and a screen of other mutants showing a similar genetic interaction revealed that Golgi targeting of Rud3p also requires Erv14p, a cargo receptor that cycles between the endoplasmic reticulum and Golgi. The one human protein with a GRAB domain, GMAP-210 (CEV14/Trip11/Trip230), is known to be on the cis-Golgi, but the COOH-terminal region that contains the GRAB domain has been reported to bind to centrosomes and gamma-tubulin (Rios, R.M, A. Sanchis, A.M. Tassin, C. Fedriani, and M. Bornens. 2004. Cell. 118:323-335). In contrast, we find that this region binds to the Golgi in a GRAB domain-dependent manner, suggesting that GMAP-210 may not link the Golgi to gamma-tubulin and centrosomes.

Indexed as

ADP-Ribosylation Factor 1Amino Acid MotifsAmino Acid SequenceAnimalsCarrier ProteinsChromatographyCOS CellsCytoskeletal ProteinsEndoplasmic ReticulumGene DeletionGenotypeGolgi ApparatusGTP PhosphohydrolasesGuanosine DiphosphateMembrane ProteinsMicroscopy, ConfocalADP-Ribosylation Factor 1Carrier ProteinsCytoskeletal ProteinsErv14 protein, S cerevisiaeGTP PhosphohydrolasesGuanosine DiphosphateMembrane ProteinsMicrotubule-Associated ProteinsMonomeric GTP-Binding ProteinsNuclear ProteinsRecombinant ProteinsRUD3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTRIP11 protein, humanTubulinVesicular Transport ProteinsYPT6 protein, S cerevisiae

Identifiers

PMID15504911
PMCPMC2172552
OpenAlexW2117938260

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.