Evidence map›Paper›PMID 12857874›Full record

ArticleMolecular biology of the cell2003

Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout.

Gilles R X Hickson, Johanne Matheson, Blake Riggs, Valerie H Maier, Andrew B Fielding, Rytis Prekeris, William Sullivan, Francis A Barr, Gwyn W Gould

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing 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

66 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
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  11. Article
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  13. Article
  14. Cytokinesis in animal cells.Cold Spring Harbor perspectives in biology · 2015
    Review
  15. Article
  16. Review
  17. Article
  18. Membrane dynamics during cytokinesis.Current opinion in cell biology · 2013
    Review
  19. Review
  20. ARF6 directs axon transport and traffic of integrins and regulates axon growth in adult DRG neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article

6 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

9 authors at 3 institutions in 2 countries.

Gilles R X HicksonThe Henry Wellcome Laboratory of Cell Biology, Division of Biochemistry and Molecular Biology, Faculty of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland.
Johanne Matheson
Blake Riggs
Valerie H Maier
Andrew B Fielding
Rytis Prekeris
William Sullivan
Francis A Barr
Gwyn W Gould
University of Glasgow · GBUniversity of California, Santa Cruz · USUniversity of Colorado Health · US

Funding

CYTOKINESIS IN THE EARLY DROSOPHILA EMBRYOR01GM046409 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI SULLIVAN, WILLIAM T. · 1997 to 2014
$4.7M
DROSOPHILA EMBRYONIC NUCLEAR DIVISION MUTATIONSR29GM046409 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI SULLIVAN, WILLIAM T. · 1991 to 1995
–
NIGMS NIH HHS GM-46409NIGMS NIH HHS R01 GM046409Wellcome Trust
6 · The paper itself

Abstract

Arfophilin is an ADP ribosylation factor (Arf) binding protein of unknown function. It is identical to the Rab11 binding protein eferin/Rab11-FIP3, and we show it binds both Arf5 and Rab11. We describe a related protein, arfophilin-2, that interacts with Arf5 in a nucleotide-dependent manner, but not Arf1, 4, or 6 and also binds Rab11. Arfophilin-2 localized to a perinuclear compartment, the centrosomal area, and focal adhesions. The localization of arfophilin-2 to the perinuclear compartment was selectively blocked by overexpression of Arf5-T31N. In contrast, a green fluorescent protein-arfophilin-2 chimera or arfophilin-2 deletions were localized around the centrosome in a region that was also enriched for transferrin receptors and Rab11 but not early endosome markers, suggesting that the distribution of the endosomal recycling compartment was altered. The arfophilins belong to a conserved family that includes Drosophila melanogaster nuclear fallout, a centrosomal protein required for cellularization. Expression of green fluorescent protein-nuclear fallout in HeLa cells resulted in a similar phenotype, indicative of functional homology and thus implicating the arfophilins in mitosis/cytokinesis. We suggest that the novel dual GTPase-binding capacity of the arfophilins could serve as an interface of signals from Rab and Arf GTPases to regulate membrane traffic and integrate distinct signals in the late endosomal recycling compartment.

Indexed as

ADP-Ribosylation FactorsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCentrosomeCHO CellsCloning, MolecularCricetinaeCricetulusDrosophila ProteinsEndosomesHeLa CellsHumansMitosisMolecular Sequence DataADP-Ribosylation FactorsarfophilinCarrier ProteinsDrosophila ProteinsNuclear Proteinsnuf protein, DrosophilaRAB11FIP3 protein, humanrab11 GTP-Binding Proteinsrab GTP-Binding Proteins

Identifiers

PMID12857874
PMCPMC165686
OpenAlexW2151140160

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.