Evidence map›Paper›PMID 22573888›Full record

ArticleMolecular biology of the cell2012

ARAP1 regulates the ring size of circular dorsal ruffles through Arf1 and Arf5.

Junya Hasegawa, Kazuya Tsujita, Tadaomi Takenawa, Toshiki Itoh

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Membrane Ruffles: Composition, Function, Formation and Visualization.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Arap1 Deficiency Causes Photoreceptor Degeneration in Mice.Investigative ophthalmology & visual science · 2017
    Article
  14. Review
  15. Regulators and Effectors of Arf GTPases in Neutrophils.Journal of immunology research · 2015
    Review
  16. Article
  17. Article
  18. Components of the CtBP1/BARS-dependent fission machinery.Histochemistry and cell biology · 2013
    Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Junya HasegawaDivision of Membrane Biology, Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kobe, Hyogo, Japan.
Kazuya Tsujita
Tadaomi Takenawa
Toshiki Itoh
Kobe University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small guanosine triphosphatase (GTPase) ADP-ribosylation factors (Arfs) regulate membrane traffic and actin reorganization under the strict control of GTPase-activating proteins (GAPs). ARAP1 (Arf GAP with Rho GAP domain, ankyrin repeat, and PH domain 1) is an Arf GAP molecule with multiple PH domains that recognize phosphatidylinositol 3,4,5-trisphosphate. We found that growth factor stimulation induced localization of ARAP1 to an area of the plasma membrane inside the ring structure of circular dorsal ruffles (CDRs). Moreover, expression of ARAP1 increased the size of the CDR filamentous-actin ring in an Arf GAP activity-dependent manner, whereas smaller CDRs were formed by ARAP1 knockdown. In addition, expression of a dominant-negative mutant of Arf1 and Arf5, the substrates of ARAP1, expanded the size of CDRs, suggesting that the two Arf isoforms regulate ring structure downstream of ARAP1. Therefore our results reveal a novel molecular mechanism of CDR ring size control through the ARAP1-Arf1/5 pathway.

Indexed as

ADP-Ribosylation Factor 1ADP-Ribosylation FactorsAnimalsBecaplerminCarrier ProteinsCell Membrane StructuresGene Knockdown TechniquesGTPase-Activating ProteinsHeLa CellsHumansMiceNIH 3T3 CellsPinocytosisProtein Structure, TertiaryProtein TransportProto-Oncogene Proteins c-sisADP-Ribosylation Factor 1ADP-Ribosylation FactorsARAP1 protein, humanARF5 protein, humanBecaplerminCarrier ProteinsGTPase-Activating ProteinsProto-Oncogene Proteins c-sis

Identifiers

PMID22573888
PMCPMC3386212
OpenAlexW2123908853

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.