Evidence map›Paper›PMID 9927415›Full record

ArticleThe EMBO journal1999

Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function.

P P Poon, D Cassel, A Spang, M Rotman, E Pick, R A Singer, G C Johnston

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

89 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Arfs on the Golgi: four conductors, one orchestra.Frontiers in molecular biosciences · 2025
    Review
  6. StaufenC facilitates utilization of the ERAD pathway to transport dsRNA through the endoplasmic reticulum to the cytosol.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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29 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

7 authors at 1 institution in 1 country.

P P PoonDepartment of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7.
D Cassel
A Spang
M Rotman
E Pick
R A Singer
G C Johnston
Dalhousie University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ARF proteins, which mediate vesicular transport, have little or no intrinsic GTPase activity. They rely on the actions of GTPase-activating proteins (GAPs) for their function. The in vitro GTPase activity of the Saccharomyces cerevisiae ARF proteins Arf1 and Arf2 is stimulated by the yeast Gcs1 protein, and in vivo genetic interactions between arf and gcs1 mutations implicate Gcs1 in vesicular transport. However, the Gcs1 protein is dispensable, indicating that additional ARF GAP proteins exist. We show that the structurally related protein Glo3, which is also dispensable, also exhibits ARF GAP activity. Genetic and in vitro approaches reveal that Glo3 and Gcs1 have an overlapping essential function at the endoplasmic reticulum (ER)-Golgi stage of vesicular transport. Mutant cells deficient for both ARF GAPs cannot proliferate, undergo a dramatic accumulation of ER and are defective for protein transport between ER and Golgi. The glo3Delta and gcs1Delta single mutations each interact with a sec21 mutation that affects a component of COPI, which mediates vesicular transport within the ER-Golgi shuttle, while increased dosage of the BET1, BOS1 and SEC22 genes encoding members of a v-SNARE family that functions within the ER-Golgi alleviates the effects of a glo3Delta mutation. An in vitro assay indicates that efficient retrieval from the Golgi to the ER requires these two proteins. These findings suggest that Glo3 and Gcs1 ARF GAPs mediate retrograde vesicular transport from the Golgi to the ER.

Indexed as

GTPase-Activating ProteinsSaccharomyces cerevisiae ProteinsADP-Ribosylation Factor 1ADP-Ribosylation FactorsAnimalsBiological Transport, ActiveDNA-Binding ProteinsEndoplasmic ReticulumEscherichia coliFungal ProteinsGenes, FungalGolgi ApparatusGTP-Binding ProteinsMutationRecombinant ProteinsSaccharomyces cerevisiaeADP-Ribosylation Factor 1ADP-Ribosylation FactorsDNA-Binding ProteinsFungal ProteinsGCS1 protein, S cerevisiaeGTPase-Activating ProteinsGTP-Binding ProteinsRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID9927415
PMCPMC1171148
OpenAlexW2033053971

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.