Evidence map›Paper›PMID 11294905›Full record

ArticleMolecular biology of the cell2001

The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum.

A Spang, J M Herrmann, S Hamamoto, R Schekman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

40 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  8. Arf1 orchestrates Rab GTPase conversion at theMolecular biology of the cell · 2021
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  9. Article
  10. The p24 Complex Contributes to Specify Arf1 for COPI Coat Selection.International journal of molecular sciences · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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  17. Article
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  19. Article
  20. A three-stage model of Golgi structure and function.Histochemistry and cell biology · 2013
    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

4 authors at 1 institution in 2 countries.

A SpangFriedrich Miescher Laboratorium, Max Planck Gesellschaft, D-72076 Tübingen, Germany. anne_spang@tuebingen.de
J M Herrmann
S Hamamoto
R Schekman
Howard Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activation of the small ras-like GTPase Arf1p requires the action of guanine nucleotide exchange factors. Four Arf1p guanine nucleotide exchange factors have been identified in yeast: Sec7p, Syt1p, Gea1p, and its homologue Gea2p. We identified GEA2 as a multicopy suppressor of a sec21-3 temperature-sensitive mutant. SEC21 encodes the gamma-subunit of coatomer, a heptameric protein complex that together with Arf1p forms the COPI coat. GEA1 and GEA2 have at least partially overlapping functions, because deletion of either gene results in no obvious phenotype, whereas the double null mutant is inviable. Conditional mutants defective in both GEA1 and GEA2 accumulate endoplasmic reticulum and Golgi membranes under restrictive conditions. The two genes do not serve completely overlapping functions because a Deltagea1 Deltaarf1 mutant is not more sickly than a Deltaarf1 strain, whereas Deltagea2 Deltaarf1 is inviable. Biochemical experiments revealed similar distributions and activities for the two proteins. Gea1p and Gea2p exist both in membrane-bound and in soluble forms. The membrane-bound forms, at least one of which, Gea2p, can be visualized on Golgi structures, are both required for vesicle budding and protein transport from the Golgi to the endoplasmic reticulum. In contrast, Sec7p, which is required for protein transport within the Golgi, is not required for retrograde protein trafficking.

Indexed as

Saccharomyces cerevisiae ProteinsADP-Ribosylation FactorsBiological Transport, ActiveCOP-Coated VesiclesEndoplasmic ReticulumFungal ProteinsGolgi ApparatusGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsIntracellular MembranesReceptors, Cell SurfaceR-SNARE ProteinsSaccharomyces cerevisiaeTemperatureADP-Ribosylation FactorsFungal ProteinsGEA1 protein, S cerevisiaeGEA2 protein, S cerevisiaeGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsReceptors, Cell SurfaceR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSec22 protein, S cerevisiaeSEC23 protein, S cerevisiae

Identifiers

PMID11294905
PMCPMC32285
OpenAlexW2105782873

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.