Evidence map›Paper›PMID 30427759›Full record

ArticleMolecular biology of the cell2019

ADP-ribosylation factor-like 4A interacts with Robo1 to promote cell migration by regulating Cdc42 activation.

Tsai-Shin Chiang, Ming-Chieh Lin, Meng-Chen Tsai, Chieh-Hsin Chen, Li-Ting Jang, Fang-Jen S Lee

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Decoding Rho GTPase signalling networks in directed cell migration.Frontiers in cell and developmental biology · 2026
    Review
  3. Review
  4. Article
  5. Thyroid cancer prognostic biomarker ARL4A and its relationship with immune infiltration.International journal of clinical and experimental pathology · 2024
    Article
  6. Science advances · 2023
    Article
  7. Article
  8. 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
  9. Article
  10. Article
  11. 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

6 authors at 1 institution in 1 country.

Tsai-Shin ChiangInstitute of Molecular Medicine, National Taiwan University, Taipei 10002, Taiwan.
Ming-Chieh LinInstitute of Molecular Medicine, National Taiwan University, Taipei 10002, Taiwan.
Meng-Chen TsaiInstitute of Molecular Medicine, National Taiwan University, Taipei 10002, Taiwan.
Chieh-Hsin ChenInstitute of Molecular Medicine, National Taiwan University, Taipei 10002, Taiwan.
Li-Ting JangInstitute of Molecular Medicine, National Taiwan University, Taipei 10002, Taiwan.
Fang-Jen S LeeInstitute of Molecular Medicine, National Taiwan University, Taipei 10002, Taiwan.
National Taiwan University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell migration is a highly regulated event that is initiated by cell membrane protrusion and actin reorganization. Robo1, a single-pass transmembrane receptor, is crucial for neuronal guidance and cell migration. ADP-ribosylation factor (Arf)-like 4A (Arl4A), an Arf small GTPase, functions in cell morphology, cell migration, and actin cytoskeleton remodeling; however, the molecular mechanisms of Arl4A in cell migration are unclear. Here, we report that the binding of Arl4A to Robo1 modulates cell migration by promoting Cdc42 activation. We found that Arl4A interacts with Robo1 in a GTP-dependent manner and that the Robo1 amino acid residues 1394-1398 are required for this interaction. The Arl4A-Robo1 interaction is essential for Arl4A-induced cell migration and Cdc42 activation but not for the plasma membrane localization of Robo1. In addition, we show that the binding of Arl4A to Robo1 decreases the association of Robo1 with the Cdc42 GTPase-activating protein srGAP1. Furthermore, Slit2/Robo1 binding down-regulates the Arl4A-Robo1 interaction in vivo, thus attenuating Cdc42-mediated cell migration. Therefore, our study reveals a novel mechanism by which Arl4A participates in Slit2/Robo1 signaling to modulate cell motility by regulating Cdc42 activity.

Indexed as

Cell MovementADP-Ribosylation FactorsAmino Acid SequenceAnimalscdc42 GTP-Binding ProteinCell MembraneChlorocebus aethiopsCOS CellsEnzyme ActivationGTPase-Activating ProteinsGuanosine TriphosphateHEK293 CellsHeLa CellsHumansIntercellular Signaling Peptides and ProteinsModels, BiologicalADP-Ribosylation FactorsARL4A protein, humancdc42 GTP-Binding ProteinGTPase-Activating ProteinsGuanosine TriphosphateIntercellular Signaling Peptides and ProteinsNerve Tissue ProteinsReceptors, ImmunologicRoundabout ProteinsSlit Homolog 2 ProteinSRGAP1 protein, human

Identifiers

PMID30427759
PMCPMC6337904
OpenAlexW2901492518

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.