ArticleRNA (New York, N.Y.)2016
Prp8 retinitis pigmentosa mutants cause defects in the transition between the catalytic steps of splicing.
Article in RNA (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Retinitis pigmentosa-linked mutations impair the snRNA unwinding activity of SNRNP200 and reduce pre-mRNA binding of PRPF8.Cellular and molecular life sciences : CMLS · 2025Article
- Reporting a Homozygous Case of Neurodevelopmental Disorder Associated With a Novel PRPF8 Variant.Molecular genetics & genomic medicine · 2025Article
- Research Progress on the Relationship Between PRPF8 and Cancer.Current issues in molecular biology · 2025Review
- Addressing the tissue specificity of U5 snRNP spliceosomopathies.Frontiers in cell and developmental biology · 2025Article
- PRPF8-mediated dysregulation of hBrr2 helicase disrupts human spliceosome kinetics and 5´-splice-site selection causing tissue-specific defects.Nature communications · 2024Article
- Regulation and mechanisms of action of RNA helicases.RNA biology · 2024Review
- Biochemical and genetic evidence supports Fyv6 as a second-step splicing factor inRNA (New York, N.Y.) · 2023Article
- Pre-mRNA splicing-associated diseases and therapies.RNA biology · 2023Review
- Structural and functional investigation of the human snRNP assembly factor AAR2 in complex with the RNase H-like domain of PRPF8.Acta crystallographica. Section D, Structural biology · 2022Article
- The Role of the U5 snRNP in Genetic Disorders and Cancer.Frontiers in genetics · 2021Review
- Pre-mRNA Processing Factors and Retinitis Pigmentosa: RNA Splicing and Beyond.Frontiers in cell and developmental biology · 2021Review
- ADisease models & mechanisms · 2020Article
- A Snu114-GTP-Prp8 module forms a relay station for efficient splicing in yeast.Nucleic acids research · 2020Article
- Spliceosomal Prp8 intein at the crossroads of protein and RNA splicing.PLoS biology · 2019Article
- Early splicing functions of fission yeast Prp16 and its unexpected requirement for gene Silencing is governed by intronic features.RNA biology · 2019Article
- Prp8 impacts cryptic but not alternative splicing frequency.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Prp8 positioning of U5 snRNA is linked to 5' splice site recognition.RNA (New York, N.Y.) · 2018Article
- Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2.Biophysical journal · 2018Article
- Structural toggle in the RNaseH domain of Prp8 helps balance splicing fidelity and catalytic efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2.Cell cycle (Georgetown, Tex.) · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Pre-mRNA splicing must occur with high fidelity and efficiency for proper gene expression. The spliceosome uses DExD/H box helicases to promote on-pathway interactions while simultaneously minimizing errors. Prp8 and Snu114, an EF2-like GTPase, regulate the activity of the Brr2 helicase, promoting RNA unwinding by Brr2 at appropriate points in the splicing cycle and repressing it at others. Mutations linked to retinitis pigmentosa (RP), a disease that causes blindness in humans, map to the Brr2 regulatory region of Prp8. Previous in vitro studies of homologous mutations in Saccharomyces cerevisiaes how that Prp8-RP mutants cause defects in spliceosome activation. Here we show that a subset of RP mutations in Prp8 also causes defects in the transition between the first and second catalytic steps of splicing. Though Prp8-RP mutants do not cause defects in splicing fidelity, they result in an overall decrease in splicing efficiency. Furthermore, genetic analyses link Snu114 GTP/GDP occupancy to Prp8-dependent regulation of Brr2. Our results implicate the transition between the first and second catalytic steps as a critical place in the splicing cycle where Prp8-RP mutants influence splicing efficiency. The location of the Prp8-RP mutants, at the "hinge" that links the Prp8 Jab1-MPN regulatory "tail" to the globular portion of the domain, suggests that these Prp8-RP mutants inhibit regulated movement of the Prp8 Jab1/MPN domain into the Brr2 RNA binding channel to transiently inhibit Brr2. Therefore, in Prp8-linked RP, disease likely results not only from defects in spliceosome assembly and activation, but also because of defects in splicing catalysis.
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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.