ArticleHuman molecular genetics2016
Prenylated retinal ciliopathy protein RPGR interacts with PDE6δ and regulates ciliary localization of Joubert syndrome-associated protein INPP5E.
Article in Human molecular genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 34 citations in OpenAlex.
- Loss of RPGR disrupts motile cilia and causes primary ciliary dyskinesia by affecting F-actin dynamics.The Journal of clinical investigation · 2026Article
- Advances in RPGR gene therapy for X‑linked retinitis pigmentosa: From preclinical insights to clinical application (Review).International journal of molecular medicine · 2026Review
- Sub-ciliary localization of CEP290 and effects of its loss in mouse photoreceptors during development.Journal of cell science · 2025Article
- Post-Translational Modifications in Cilia and Ciliopathies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Ciliopathy-associated protein, CEP290, is required for ciliary necklace and outer segment membrane formation in retinal photoreceptors.bioRxiv : the preprint server for biology · 2025Article
- Regulation of INPP5E in Ciliogenesis, Development, and Disease.International journal of biological sciences · 2025Review
- Updates on protein-prenylation and associated inherited retinopathies.Frontiers in ophthalmology · 2024Review
- Identification of a novelFrontiers in pediatrics · 2024Article
- Clinical characteristics of high myopia in female carriers of pathogenicOphthalmic genetics · 2023Review
- Impaired glutamylation of RPGRProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Composition, organization and mechanisms of the transition zone, a gate for the cilium.EMBO reports · 2022Review
- Article
- The Major Ciliary Isoforms of RPGR Build Different Interaction Complexes with INPP5E and RPGRIP1L.International journal of molecular sciences · 2021Article
- RPGR isoform imbalance causes ciliary defects due to exon ORF15 mutations in X-linked retinitis pigmentosa (XLRP).Human molecular genetics · 2021Article
- Compartmentalization of Photoreceptor Sensory Cilia.Frontiers in cell and developmental biology · 2021Review
- Translational Read-Through Therapy ofInternational journal of molecular sciences · 2020Article
- Review
- A novel missense variant c.G644A (p.G215E) of the RPGR gene in a Chinese family causes X-linked retinitis pigmentosa.Bioscience reports · 2019Article
- Balancing the Photoreceptor Proteome: Proteostasis Network Therapeutics for Inherited Retinal Disease.Genes · 2019Review
- Disruption of RPGR protein interaction network is the common feature of RPGR missense variations that cause XLRP.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
5 authors.
Funding
Abstract
Ciliary trafficking defects underlie the pathogenesis of severe human ciliopathies, including Joubert Syndrome (JBTS), Bardet-Biedl Syndrome, and some forms of retinitis pigmentosa (RP). Mutations in the ciliary protein RPGR (retinitis pigmentosa GTPase regulator) are common causes of RP-associated photoreceptor degeneration worldwide. While previous work has suggested that the localization of RPGR to cilia is critical to its functions, the mechanism by which RPGR and its associated cargo are trafficked to the cilia is unclear. Using proteomic and biochemical approaches, we show that RPGR interacts with two JBTS-associated ciliary proteins: PDE6δ (delta subunit of phosphodiesterase; a prenyl-binding protein) and INPP5E (inositol polyphosphate-5-phosphatase 5E). We find that PDE6δ binds selectively to the C-terminus of RPGR and that this interaction is critical for RPGR’s localization to cilia. Furthermore, we show that INPP5E associates with the N-terminus of RPGR and trafficking of INPP5E to cilia is dependent upon the ciliary localization of RPGR. These results implicate prenylation of RPGR as a critical modification for its localization to cilia and, in turn suggest that trafficking of INPP5E to cilia depends upon the interaction of RPGR with PDE6δ. Finally, our results implicate INPP5E, a novel RPGR-interacting protein, in the pathogenesis of RPGR-associated ciliopathies.
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