ArticleJournal of cell science2011
Localization of retinitis pigmentosa 2 to cilia is regulated by Importin beta2.
Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 101 citations in OpenAlex.
- Rab8 and TNPO1 function as the ciliary transport adapters for GPCRs.The Journal of biological chemistry · 2026Article
- Article
- Importin α regulates ciliogenesis and cilia length with implications for Xenopus nephrogenesis.Journal of cell science · 2025Article
- A tale of Rabs and the exocyst complex in ciliary trafficking and biogenesis.Frontiers in cell and developmental biology · 2025Review
- TBCC Domain-Containing Protein Regulates Sporulation and Virulence ofInternational journal of molecular sciences · 2024Article
- Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024Review
- Transport and barrier mechanisms that regulate ciliary compartmentalization and ciliopathies.Nature reviews. Nephrology · 2024Review
- Bardet-Biedl syndrome: The pleiotropic role of the chaperonin-like BBS6, 10, and 12 proteins.American journal of medical genetics. Part C, Seminars in medical genetics · 2022Review
- Non-transport roles of nuclear import receptors: In need of the right balance.Frontiers in cell and developmental biology · 2022Review
- TNPO2 variants associate with human developmental delays, neurologic deficits, and dysmorphic features and alter TNPO2 activity in Drosophila.American journal of human genetics · 2021Article
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- ARL3, a small GTPase with a functionally conserved role in primary cilia and immune synapses.Small GTPases · 2021Review
- Zebrafish Models of Photoreceptor Dysfunction and Degeneration.Biomolecules · 2021Review
- Transportin-1: A Nuclear Import Receptor with Moonlighting Functions.Frontiers in molecular biosciences · 2021Review
- Lipid Modifications in Cilia Biology.Journal of clinical medicine · 2019Review
- Influenza virus uses transportin 1 for vRNP debundling during cell entry.Nature microbiology · 2019Article
- NPHP proteins are binding partners of nucleoporins at the base of the primary cilium.PloS one · 2019Article
- Newly synthesized polycystin-1 takes different trafficking pathways to the apical and ciliary membranes.Traffic (Copenhagen, Denmark) · 2018Article
- NUP98 Sets the Size-Exclusion Diffusion Limit through the Ciliary Base.Current biology : CB · 2018Article
- Gene therapy for the treatment of X-linked retinitis pigmentosa.Expert opinion on orphan drugs · 2018Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ciliopathies represent a newly emerging group of human diseases that share a common etiology resulting from dysfunction of the cilium or centrosome. The gene encoding the retinitis pigmentosa 2 protein (RP2) is mutated in X-linked retinitis pigmentosa. RP2 localizes to the ciliary base and this requires the dual acylation of the N-terminus, but the precise mechanism by which RP2 is trafficked to the cilia is unknown. Here we have characterized an interaction between RP2 and Importin β2 (transportin-1), a member of the Importin-β family that regulates nuclear-cytoplasmic shuttling. We demonstrate that Importin β2 is necessary for localization of RP2 to the primary cilium because ablation of Importin β2 by shRNA blocks entry both of endogenous and exogenous RP2 to the cilium. Furthermore, we identify two distinct binding sites of RP2, which interact independently with Importin β2. One binding site is a nuclear localization signal (NLS)-like sequence that is located at the N-terminus of RP2 and the other is an M9-like sequence within the tubulin folding cofactor C (TBCC) domain. Mutation of the NLS-like consensus sequence did not abolish localization of RP2 to cilia, suggesting that the sequence is not essential for RP2 ciliary targeting. Interestingly, we found that several missense mutations that cause human disease fall within the M9-like sequence of RP2 and these mutations block entry of RP2 into the cilium, as well as its interaction with Importin β2. Together, this work further highlights a role of Importin β2 in regulation of the entry of RP2 and other proteins into the ciliary compartment.
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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.