Evidence map›Paper›PMID 19299515›Full record

ArticleThe Journal of biological chemistry2009

Three homologous ArfGAPs participate in coat protein I-mediated transport.

Akina Saitoh, Hye-Won Shin, Akane Yamada, Satoshi Waguri, Kazuhisa Nakayama

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
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  8. Article
  9. ArfGAPs: key regulators for receptor sorting.Receptors & clinical investigation · 2014
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. COPI budding within the Golgi stack.Cold Spring Harbor perspectives in biology · 2011
    Review
  17. Article
  18. Article
  19. Article
  20. Models for the functions of Arf GAPs.Seminars in cell & developmental biology · 2011
    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

5 authors at 2 institutions in 1 country.

Akina SaitohGraduate School of Pharmaceutical Sciences and Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.
Hye-Won ShinGraduate School of Pharmaceutical Sciences and Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan; Career-Path Promotion Unit for Young Life Scientists, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.
Akane YamadaDepartment of Anatomy and Histology, Fukushima Medical University, School of Medicine, Fukushima City, Fukushima 960-1295, Japan.
Satoshi WaguriDepartment of Anatomy and Histology, Fukushima Medical University, School of Medicine, Fukushima City, Fukushima 960-1295, Japan.
Kazuhisa NakayamaGraduate School of Pharmaceutical Sciences and Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. Electronic address: kazunaka@pharm.kyoto-u.ac.jp.
Kyoto University · JPFukushima Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ArfGAP1 is a prototype of GTPase-activating proteins for ADP-ribosylation factors (ARFs) and has been proposed to be involved in retrograde transport from the Golgi apparatus to the endoplasmic reticulum (ER) by regulating the uncoating of coat protein I (COPI)-coated vesicles. Depletion of ArfGAP1 by RNA interference, however, causes neither a discernible phenotypic change in the COPI localization nor a change in the Golgi-to-ER retrograde transport. Therefore, we also examined ArfGAP2 and ArfGAP3, closely related homologues of ArfGAP1. Cells in which ArfGAP1, ArfGAP2, and ArfGAP3 are simultaneously knocked down show an increase in the GTP-bound ARF level. Furthermore, in these cells proteins resident in or cycling through the cis-Golgi, including ERGIC-53, beta-COP, and GM130, accumulate in the ER-Golgi intermediate compartment, and Golgi-to-ER retrograde transport is blocked. The phenotypes observed in the triple ArfGAP knockdown cells are similar to those seen in beta-COP-depleted cells. Both the triple ArfGAP- and beta-COP-depleted cells accumulate characteristic vacuolar structures that are visible under electron microscope. Furthermore, COPI is concentrated at rims of the vacuolar structures in the ArfGAP-depleted cells. On the basis of these observations, we conclude that ArfGAP1, ArfGAP2, and ArfGAP3 have overlapping roles in regulating COPI function in Golgi-to-ER retrograde transport.

Indexed as

AutoantigensBiological TransportCoatomer ProteinCOP-Coated VesiclesEndoplasmic ReticulumGene Knockdown TechniquesGolgi ApparatusGTPase-Activating ProteinsHeLa CellsHumansMannose-Binding LectinsMembrane ProteinsVacuolesAutoantigensCoatomer ProteinGolgin subfamily A member 2GTPase-Activating ProteinsLMAN1 protein, humanMannose-Binding LectinsMembrane Proteins

Identifiers

PMID19299515
PMCPMC2679494
OpenAlexW2118410051

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.