ArticleHuman molecular genetics2018
Oligomerization of Prph2 and Rom1 is essential for photoreceptor outer segment formation.
Article in Human molecular genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 56 citations in OpenAlex.
- Advancing genetic pathogenicity prediction with three-dimensional proteoform-phenotype analysis.medRxiv : the preprint server for health sciences · 2026Article
- Ciliary Defects in Inherited Retinal Diseases.Advanced genetics (Hoboken, N.J.) · 2026Review
- Prime editing for the investigation of aberrant splicing defect associated with a pathogenicMolecular therapy. Nucleic acids · 2025Article
- Genotype-Phenotype Correlations inGenes · 2025Article
- Clearing the AIR: AAmerican journal of ophthalmology case reports · 2025Article
- The PRPH2 D2 Loop: Biochemical Insights and Implications in Disease.Advances in experimental medicine and biology · 2025Review
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- Digenic Inheritance in Rare Disorders and Mitochondrial Disease-Crossing the Frontier to a More Comprehensive Understanding of Etiology.International journal of molecular sciences · 2024Review
- Article
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- Prph2 knock-in mice recapitulate human central areolar choroidal dystrophy retinal degeneration and exhibit aberrant synaptic remodeling and microglial activation.Cell death & disease · 2023Article
- ROM1 is redundant to PRPH2 as a molecular building block of photoreceptor disc rims.bioRxiv : the preprint server for biology · 2023Article
- Primary versus Secondary Elevations in Fundus Autofluorescence.International journal of molecular sciences · 2023Review
- Comparative study of PRPH2 D2 loop mutants reveals divergent disease mechanism in rods and cones.Cellular and molecular life sciences : CMLS · 2023Article
- Photoreceptor disc incisures form as an adaptive mechanism ensuring the completion of disc enclosure.eLife · 2023Article
- Photoreceptor disc incisures form as an adaptive mechanism ensuring the completion of disc enclosure.bioRxiv : the preprint server for biology · 2023Article
- The Role of Peripherin-2/ROM1 Complexes in Photoreceptor Outer Segment Disc Morphogenesis.Advances in experimental medicine and biology · 2023Article
- Multimodal Study ofDiagnostics (Basel, Switzerland) · 2022Article
- Delineating the Clinical Phenotype of Patients With the c.629C>G, p.Pro210Arg Mutation in Peripherin-2.Investigative ophthalmology & visual science · 2022Article
- Genetic dissection of non-syndromic retinitis pigmentosa.Indian journal of ophthalmology · 2022Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Mutations in peripherin 2 (PRPH2, also known as Rds), a tetraspanin protein found in photoreceptor outer segments (OSs), cause retinal degeneration ranging from rod-dominant retinitis pigmentosa (RP) to cone-dominant macular dystrophy (MD). Understanding why some Prph2 mutants affect rods while others affect cones remains a critical unanswered question. Prph2 is essential for OS structure and function and exhibits a very specific pattern of oligomerization with its homolog Rom1. Non-covalent Prph2/Rom1 homo- and hetero-tetramers assemble into higher-order covalently linked complexes held together by an intermolecular disulfide bond at Prph2-C150/Rom1-C153. Here we disrupt this crucial bond using a C150S-Prph2 knockin mouse line to study the role of Prph2 higher-order complex formation. We find that C150S-Prph2 traffics to the OS, interacts with Rom1 and forms non-covalent tetramers, but alone cannot support normal OS structure and function. However, C150S-Prph2 supports the initiation or elaboration of OS disc structures, and improves rod OS ultrastructure in the presence of wild-type (WT) Prph2 (i.e. Prph2C150S/+ versus Prph2+/-). Prph2C150S/+ animals exhibit haploinsufficiency in rods, but a dominant-negative phenotype in cones, suggesting cones have a different requirement for large Prph2 complexes than rods. Importantly, cone but not rod function can be improved by the addition of one Prph2Y141C allele, a mutation responsible for pattern dystrophy owing to the extra cysteine. Combined these findings show that covalently linked Prph2 complexes are essential for OS formation, but not for Prph2 targeting to the OS, and that cones are especially sensitive to having a broad distribution of Prph2 complex types (i.e. tetramers and large complexes).
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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.