ArticleBiology open2016
RPGR, a prenylated retinal ciliopathy protein, is targeted to cilia in a prenylation- and PDE6D-dependent manner.
Article in Biology open, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Investigating G-quadruplex structures inHeliyon · 2024Article
- Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies.Nature reviews. Nephrology · 2024Review
- Algal rhodopsins encoding diverse signal sequence holds potential for expansion of organelle optogenetics.Biophysics and physicobiology · 2023Article
- Article
- Impaired glutamylation of RPGRProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Human iPSC-Derived Retinal Organoids and Retinal Pigment Epithelium for Novel IntronicJournal of personalized medicine · 2022Article
- Identification of a novel RPGR mutation associated with X-linked cone-rod dystrophy in a Chinese family.BMC ophthalmology · 2021Article
- Interaction of INPP5E with ARL13B is essential for its ciliary membrane retention but dispensable for its ciliary entry.Biology open · 2021Article
- The Primary Cilium as a Therapeutic Target in Ocular Diseases.Frontiers in pharmacology · 2020Review
- A novel missense variant c.G644A (p.G215E) of the RPGR gene in a Chinese family causes X-linked retinitis pigmentosa.Bioscience reports · 2019Article
- Lipid Modifications in Cilia Biology.Journal of clinical medicine · 2019Review
- Article
- Role of oxidative stress in Retinitis pigmentosa: new involved pathways by an RNA-Seq analysis.Cell cycle (Georgetown, Tex.) · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
RPGR (retinitis pigmentosa GTPase regulator) is a ciliary protein associated with several forms of inherited retinal degenerative diseases. PDE6D is a ubiquitously expressed prenyl-binding protein and involved in ciliary targeting of prenylated proteins. The current working model for the RPGR function depicts that RPGR acts as a scaffold protein to recruit cargo-loaded PDE6D to primary cilia. Here, we present evidence demonstrating an alternative relationship between RPGR and PDE6D, in which RPGR is a cargo of PDE6D for ciliary targeting. We found that the constitutive isoform of RPGR, which is prenylated, requires prenylation for its ciliary localization. We also found that there are at least two independent ciliary targeting signals in RPGR: one within the N-terminal region that contains the RCC1-like domain and the other near the prenylation site at the C-terminus. Ablation of PDE6D blocked ciliary targeting of RPGR. Our study indicates that prenylated RPGR is one of the cargos of PDE6D for ciliary trafficking and provides insight into the mechanisms by which RPGR is targeted to cilia.
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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.