ArticleMolecular biology of the cell2017
ADP-ribosylation factor-like 4C binding to filamin-A modulates filopodium formation and cell migration.
Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 32 citations in OpenAlex.
- 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 · 2026Article
- ARHGAP21 enhances metastasis in hepatocellular carcinoma by inhibiting ubiquitination of filamin A.Cell death discovery · 2026Article
- Phosphatidylinositol 4,5-bisphosphate mediates Arl4D self-interaction to promote Pak1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Endothelial tip-cell position, filopodia formation and biomechanics require BMPR2 expression and signaling.Communications biology · 2025Article
- The potential of ARL4C and its-mediated genes in atherosclerosis and agent development.Frontiers in pharmacology · 2025Review
- Small GTPase ARL4C Associated with Various Cancers Affects Microtubule Nucleation.Biomedicines · 2024Article
- Ursolic acid inhibits the metastasis of colon cancer by downregulating ARL4C expression.Oncology reports · 2024Article
- Interaction of LARP4 to filamin A mechanosensing domain regulates cell migrations.Frontiers in cell and developmental biology · 2023Article
- 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 · 2022Article
- Filamin A Is a Potential Driver of Breast Cancer MetastasisFrontiers in oncology · 2022Article
- Loss of YY1, a Regulator of Metabolism in Melanoma, Drives Melanoma Cell Invasiveness and Metastasis Formation.Frontiers in cell and developmental biology · 2022Article
- Proteomic Analysis of Extracellular Vesicles FromFrontiers in cellular and infection microbiology · 2022Article
- LXN deficiency regulates cytoskeleton remodelling by promoting proteolytic cleavage of Filamin A in vascular endothelial cells.Journal of cellular and molecular medicine · 2021Article
- Wnt/Beta-catenin/Esrrb signalling controls the tissue-scale reorganization and maintenance of the pluripotent lineage during murine embryonic diapause.Nature communications · 2020Article
- RYK-mediated filopodial pathfinding facilitates midgut elongation.Development (Cambridge, England) · 2020Article
- Review
- Arl4D-EB1 interaction promotes centrosomal recruitment of EB1 and microtubule growth.Molecular biology of the cell · 2020Article
- CRL5-dependent regulation of the small GTPases ARL4C and ARF6 controls hippocampal morphogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- ARL4C is associated with initiation and progression of lung adenocarcinoma and represents a therapeutic target.Cancer science · 2020Article
- The Role of ARF Family Proteins and Their Regulators and Effectors in Cancer Progression: A Therapeutic Perspective.Frontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Changes in cell morphology and the physical forces that occur during migration are generated by a dynamic filamentous actin cytoskeleton. The ADP-ribosylation factor-like 4C (Arl4C) small GTPase acts as a molecular switch to regulate morphological changes and cell migration, although the mechanism by which this occurs remains unclear. Here we report that Arl4C functions with the actin regulator filamin-A (FLNa) to modulate filopodium formation and cell migration. We found that Arl4C interacted with FLNa in a GTP-dependent manner and that FLNa IgG repeat 22 is both required and sufficient for this interaction. We also show that interaction between FLNa and Arl4C is essential for Arl4C-induced filopodium formation and increases the association of FLNa with Cdc42-GEF FGD6, promoting cell division cycle 42 (Cdc42) GTPase activation. Thus our study revealed a novel mechanism, whereby filopodium formation and cell migration are regulated through the Arl4C-FLNa-mediated activation of Cdc42.
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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.