Evidence map›Paper›PMID 11756474›Full record

ArticleThe Journal of cell biology2001

The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network.

P P Poon, S F Nothwehr, R A Singer, G C Johnston

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

43 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024
    Review
  4. Article
  5. Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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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

4 authors at 2 institutions in 2 countries.

P P PoonDepartment of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7.
S F Nothwehr
R A Singer
G C Johnston
Dalhousie University · CAUniversity of Missouri · US

Funding

ANALYSIS OF GOLGI MEMBRANE PROTEIN LOCALIZATION IN YEASTR01GM053449 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI NOTHWEHR, STEVEN F · 2000 to 2003
$749k
YEAST LATE GOLGI MEMBRANE PROTEIN RETENTIONR29GM053449 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI NOTHWEHR, STEVEN F · 1995 to 1999
–
NIGMS NIH HHS GM53449NIGMS NIH HHS R01 GM053449NIGMS NIH HHS R29 GM053449
6 · The paper itself

Abstract

Many intracellular vesicle transport pathways involve GTP hydrolysis by the ADP-ribosylation factor (ARF) type of monomeric G proteins, under the control of ArfGAP proteins. Here we show that the structurally related yeast proteins Gcs1 and Age2 form an essential ArfGAP pair that provides overlapping function for TGN transport. Mutant cells lacking the Age2 and Gcs1 proteins cease proliferation, accumulate membranous structures resembling Berkeley bodies, and are unable to properly process and localize the vacuolar hydrolase carboxypeptidase (CPY) and the vacuolar membrane protein alkaline phosphatase (ALP), which are transported from the TGN to the vacuole by distinct transport routes. Immunofluorescence studies localizing the proteins ALP, Kex2 (a TGN resident protein), and Vps10 (the CPY receptor for transport from the TGN to the vacuole) suggest that inadequate function of this ArfGAP pair leads to a fragmentation of TGN, with effects on secretion and endosomal transport. Our results demonstrate that the Gcs1 + Age2 ArfGAP pair provides overlapping function for transport from the TGN, and also indicate that multiple activities at the TGN can be maintained with the aid of a single ArfGAP.

Indexed as

GTPase-Activating ProteinsSaccharomyces cerevisiae ProteinsADP-Ribosylation Factorsbeta-FructofuranosidaseDNA-Binding ProteinsFungal ProteinsGenes, LethalGlycoside HydrolasesKineticsMicroscopy, ElectronModels, BiologicalProtein TransportSaccharomyces cerevisiaetrans-Golgi NetworkADP-Ribosylation FactorsAGE2 protein, S cerevisiaebeta-FructofuranosidaseDNA-Binding ProteinsFungal ProteinsGCS1 protein, S cerevisiaeGlycoside HydrolasesGTPase-Activating ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID11756474
PMCPMC2199332
OpenAlexW2094888005

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.