ArticleeLife2021
ARL3 activation requires the co-GEF BART and effector-mediated turnover.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Mechanistic insights on spatiotemporal control of Ras-signaling.Biological chemistry · 2026Review
- Molecular basis for the activation of outer dynein arms in cilia.Nature structural & molecular biology · 2025Article
- A novel recurrent ARL3 variant c.209G > A p.(Gly70Glu) causes variable non-syndromic dominant retinal dystrophy with defective lipidated protein transport in human retinal stem cell models.Human molecular genetics · 2025Article
- ARL3 GTPases facilitate ODA16 unloading from IFT in motile cilia.Science advances · 2024Article
- Characterization of the small Arabidopsis thaliana GTPase and ADP-ribosylation factor-like 2 protein TITAN 5.Journal of cell science · 2024Article
- Characterization of the smallbioRxiv : the preprint server for biology · 2024Article
- The ARF GTPase regulatory network in collective invasion and metastasis.Biochemical Society transactions · 2023Review
- RABL2 promotes the outward transition zone passage of signaling proteins in cilia via ARL3.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Disrupting the ciliary gradient of active Arl3 affects rod photoreceptor nuclear migration.eLife · 2023Article
- ARL3 mediates BBSome ciliary turnover by promoting its outward movement across the transition zone.The Journal of cell biology · 2022Article
- Loss of ARL13 impedes BBSome-dependent cargo export from Chlamydomonas cilia.The Journal of cell biology · 2022Article
- Article
- Stabilization of the RAS:PDE6D Complex Is a Novel Strategy to Inhibit RAS Signaling.Journal of medicinal chemistry · 2022Article
- ARL3 and ARL13B GTPases participate in distinct steps of INPP5E targeting to the ciliary membrane.Biology open · 2021Article
- The Structural and Biochemical Characterization of UNC119B Cargo Binding and Release Mechanisms.Biochemistry · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
The ADP-ribosylation factor-like 3 (ARL3) is a ciliopathy G-protein which regulates the ciliary trafficking of several lipid-modified proteins. ARL3 is activated by its guanine exchange factor (GEF) ARL13B via an unresolved mechanism. BART is described as an ARL3 effector which has also been implicated in ciliopathies, although the role of its ARL3 interaction is unknown. Here, we show that, at physiological GTP:GDP levels, human ARL3GDP is weakly activated by ARL13B. However, BART interacts with nucleotide-free ARL3 and, in concert with ARL13B, efficiently activates ARL3. In addition, BART binds ARL3GTP and inhibits GTP dissociation, thereby stabilising the active G-protein; the binding of ARL3 effectors then releases BART. Finally, using live cell imaging, we show that BART accesses the primary cilium and colocalises with ARL13B. We propose a model wherein BART functions as a bona fide co-GEF for ARL3 and maintains the active ARL3GTP, until it is recycled by ARL3 effectors.
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Registered trials
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.