Evidence map›Paper›PMID 25225293›Full record

ArticleThe Journal of biological chemistry2014

The Arf6 GTPase-activating proteins ARAP2 and ACAP1 define distinct endosomal compartments that regulate integrin α5β1 traffic.

Pei-Wen Chen, Ruibai Luo, Xiaoying Jian, Paul A Randazzo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

32 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Sema3dInternational journal of biological sciences · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Host Cell Signatures of the Envelopment Site within Beta-Herpes Virions.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019
    Review
  20. 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

4 authors at 1 institution in 1 country.

Pei-Wen ChenLaboratory of Cellular and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892.
Ruibai LuoLaboratory of Cellular and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892.
Xiaoying JianLaboratory of Cellular and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892.
Paul A RandazzoLaboratory of Cellular and Molecular Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892. Electronic address: randazzp@mail.nih.gov.
National Institutes of Health · US

Funding

Regulation of ADP-ribosylation factorZIABC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 2009 to 2025
$27.9M
REGULATION OF ADP-RIBOSYLATION FACTORZ01BC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 1996 to 2008
$3.3M
Intramural NIH HHS Z01 BC007365NCI NIH HHS BC 007365
6 · The paper itself

Abstract

Arf6 and the Arf6 GTPase-activating protein (GAP) ACAP1 are established regulators of integrin traffic important to cell adhesion and migration. However, the function of Arf6 with ACAP1 cannot explain the range of Arf6 effects on integrin-based structures. We propose that Arf6 has different functions determined, in part, by the associated Arf GAP. We tested this idea by comparing the Arf6 GAPs ARAP2 and ACAP1. We found that ARAP2 and ACAP1 had opposing effects on apparent integrin β1 internalization. ARAP2 knockdown slowed, whereas ACAP1 knockdown accelerated, integrin β1 internalization. Integrin β1 association with adaptor protein containing a pleckstrin homology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper motif (APPL)-positive endosomes and EEA1-positive endosomes was affected by ARAP2 knockdown and depended on ARAP2 GAP activity. ARAP2 formed a complex with APPL1 and colocalized with Arf6 and APPL in a compartment distinct from the Arf6/ACAP1 tubular recycling endosome. In addition, although ACAP1 and ARAP2 each colocalized with Arf6, they did not colocalize with each other and had opposing effects on focal adhesions (FAs). ARAP2 overexpression promoted large FAs, but ACAP1 overexpression reduced FAs. Taken together, the data support a model in which Arf6 has at least two sites of opposing action defined by distinct Arf6 GAPs.

Indexed as

Adaptor Proteins, Signal TransducingADP-Ribosylation Factor 6ADP-Ribosylation FactorsCarrier ProteinsEndocytosisEndosomesErbB ReceptorsFocal AdhesionsGTPase-Activating ProteinsHeLa CellsHumansProtein TransportReceptors, VitronectinTransferrinVesicular Transport ProteinsACAP1 protein, humanAdaptor Proteins, Signal TransducingADP-Ribosylation Factor 6ADP-Ribosylation FactorsAPPL1 protein, humanARAP2 protein, humanARF6 protein, humanCarrier Proteinsearly endosome antigen 1EGFR protein, humanErbB ReceptorsGTPase-Activating Proteinsintegrin alphavbeta1Receptors, VitronectinTransferrinVesicular Transport ProteinsACAP1ADP Ribosylation Factor (ARF)APPLARAP2EndosomeGTPase-activating Protein (GAP)IntegrinMembrane Trafficking

Identifiers

PMID25225293
PMCPMC4215208
OpenAlexW1974406469

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.