Evidence map›Paper›PMID 17804820›Full record

ArticleMolecular biology of the cell2007

ARL4D recruits cytohesin-2/ARNO to modulate actin remodeling.

Chun-Chun Li, Tsai-Chen Chiang, Tsung-Sheng Wu, Gustavo Pacheco-Rodriguez, Joel Moss, Fang-Jen S Lee

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

61 citing papers in PubMed, 101 citations in OpenAlex.

  1. Implications of ADP-Ribosylation Factor-Like Protein 4C (ARL4C) in Human Neoplasia With Special Emphasis on Ameloblastoma: A Scoping Review.Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The Arf family GTPases: Regulation of vesicle biogenesis and beyond.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  15. Article
  16. Article
  17. Phosphorylation of Arl4A/D promotes their binding by the HYPK chaperone for their stable recruitment to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Physiological and Pathological Roles of the Cytohesin Family in Neurons.International journal of molecular sciences · 2022
    Review
  20. An update on genetically encoded lipid biosensors.Molecular biology of the cell · 2022
    Article

1 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

6 authors at 2 institutions in 2 countries.

Chun-Chun LiInstitute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 100, Taiwan.
Tsai-Chen Chiang
Tsung-Sheng Wu
Gustavo Pacheco-Rodriguez
Joel Moss
Fang-Jen S Lee
National Taiwan University Hospital · TWNational Institutes of Health · US

Funding

Molecular Characterization and Regulation of GTP-binding ProteinsZIAHL000627 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI VAUGHAN, MARTHA · 2009 to 2016
$8.4M
REGULATION OF GTP-BINDING PROTEINSZ01HL000627 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI VAUGHAN, MARTHA · 1985 to 2008
$4.5M
Intramural NIH HHS
6 · The paper itself

Abstract

ARL4D is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. Although the primary structure of ARL4D is very similar to that of other ARF/ARL molecules, its function remains unclear. Cytohesin-2/ARF nucleotide-binding-site opener (ARNO) is a guanine nucleotide-exchange factor (GEF) for ARF, and, at the plasma membrane, it can activate ARF6 to regulate actin reorganization and membrane ruffling. We show here that ARL4D interacts with the C-terminal pleckstrin homology (PH) and polybasic c domains of cytohesin-2/ARNO in a GTP-dependent manner. Localization of ARL4D at the plasma membrane is GTP- and N-terminal myristoylation-dependent. ARL4D(Q80L), a putative active form of ARL4D, induced accumulation of cytohesin-2/ARNO at the plasma membrane. Consistent with a known action of cytohesin-2/ARNO, ARL4D(Q80L) increased GTP-bound ARF6 and induced disassembly of actin stress fibers. Expression of inactive cytohesin-2/ARNO(E156K) or small interfering RNA knockdown of cytohesin-2/ARNO blocked ARL4D-mediated disassembly of actin stress fibers. Similar to the results with cytohesin-2/ARNO or ARF6, reduction of ARL4D suppressed cell migration activity. Furthermore, ARL4D-induced translocation of cytohesin-2/ARNO did not require phosphoinositide 3-kinase activation. Together, these data demonstrate that ARL4D acts as a novel upstream regulator of cytohesin-2/ARNO to promote ARF6 activation and modulate actin remodeling.

Indexed as

ActinsADP-Ribosylation FactorsAnimalsCatalysisCell LineCell MembraneCell MovementChlorocebus aethiopsGTPase-Activating ProteinsGuanosine TriphosphateHumansMembrane ProteinsMutationPhosphatidylinositol 3-KinasesProtein BindingProtein TransportActinsADP-ribosylation factor related proteinsADP-Ribosylation Factorscytohesin-2GTPase-Activating ProteinsGuanosine TriphosphateMembrane ProteinsPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktTranscription Factors

Identifiers

PMID17804820
PMCPMC2043562
OpenAlexW2140660208

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.