Evidence map›Paper›PMID 20858901›Full record

ArticleThe Journal of biological chemistry2010

ARFGAP2 and ARFGAP3 are essential for COPI coat assembly on the Golgi membrane of living cells.

Fredrik Kartberg, Lennart Asp, Selma Y Dejgaard, Maria Smedh, Julia Fernandez-Rodriguez, Tommy Nilsson, John F Presley

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The origin and evolution of cell types.Nature reviews. Genetics · 2016
    Review
  8. Article
  9. Regulators and Effectors of Arf GTPases in Neutrophils.Journal of immunology research · 2015
    Review
  10. Article
  11. Article
  12. Retrograde traffic from the Golgi to the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013
    Review
  13. Article
  14. COPI budding within the Golgi stack.Cold Spring Harbor perspectives in biology · 2011
    Review
  15. 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

7 authors at 3 institutions in 2 countries.

Fredrik KartbergDepartment of Medical and Clinical Genetics, Institute of Biomedicine, University of Gothenburg, 405 30 Göteborg, Sweden.
Lennart Asp
Selma Y Dejgaard
Maria Smedh
Julia Fernandez-Rodriguez
Tommy Nilsson
John F Presley
University of Gothenburg · SEMcGill University · CAMcGill University Health Centre · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Coat protein complex I (COPI) vesicles play a central role in the recycling of proteins in the early secretory pathway and transport of proteins within the Golgi stack. Vesicle formation is initiated by the exchange of GDP for GTP on ARF1 (ADP-ribosylation factor 1), which, in turn, recruits the coat protein coatomer to the membrane for selection of cargo and membrane deformation. ARFGAP1 (ARF1 GTPase-activating protein 1) regulates the dynamic cycling of ARF1 on the membrane that results in both cargo concentration and uncoating for the generation of a fusion-competent vesicle. Two human orthologues of the yeast ARFGAP Glo3p, termed ARFGAP2 and ARFGAP3, have been demonstrated to be present on COPI vesicles generated in vitro in the presence of guanosine 5'-3-O-(thio)triphosphate. Here, we investigate the function of these two proteins in living cells and compare it with that of ARFGAP1. We find that ARFGAP2 and ARFGAP3 follow the dynamic behavior of coatomer upon stimulation of vesicle budding in vivo more closely than does ARFGAP1. Electron microscopy of ARFGAP2 and ARFGAP3 knockdowns indicated Golgi unstacking and cisternal shortening similarly to conditions where vesicle uncoating was blocked. Furthermore, the knockdown of both ARFGAP2 and ARFGAP3 prevents proper assembly of the COPI coat lattice for which ARFGAP1 does not seem to play a major role. This suggests that ARFGAP2 and ARFGAP3 are key components of the COPI coat lattice and are necessary for proper vesicle formation.

Indexed as

ADP-Ribosylation Factor 1ADP-Ribosylation FactorsCoat Protein Complex ICOP-Coated VesiclesGolgi ApparatusGTPase-Activating ProteinsGuanosine TriphosphateHeLa CellsHumansImmunoenzyme TechniquesIntracellular MembranesProtein TransportRNA, Small InterferingTranscription FactorsADP-Ribosylation Factor 1ADP-Ribosylation FactorsARFGAP2 protein, humanARFGAP3 protein, humanCoat Protein Complex IGTF2A1L protein, humanGTPase-Activating ProteinsGuanosine TriphosphateRNA, Small InterferingTranscription Factors

Identifiers

PMID20858901
PMCPMC2978600
OpenAlexW2017475690

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.