ArticleeLife2023
ROM1 is redundant to PRPH2 as a molecular building block of photoreceptor disc rims.
Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 4 citations in OpenAlex.
- Advancing genetic pathogenicity prediction with three-dimensional proteoform-phenotype analysis.medRxiv : the preprint server for health sciences · 2026Article
- The tetraspanin disc proteins, peripherin-2 and ROM1, facilitate CNG channel localization to the rod outer segment.Molecular biology of the cell · 2026Article
- Photoreceptor outer segment disk rim curvature relies on a tetraspanin interaction web.The Journal of biological chemistry · 2026Article
- Photoreceptor outer segment disk rim curvature relies on a tetraspanin interaction web.bioRxiv : the preprint server for biology · 2026Article
- Ciliary Defects in Inherited Retinal Diseases.Advanced genetics (Hoboken, N.J.) · 2026Review
- Peripherin-2 and ROM1 Incorporate Directly Into the Rims of Enclosing Photoreceptor Discs Without Accumulating in the Nascent Disc Lamellae.Investigative ophthalmology & visual science · 2025Article
- The PRPH2 D2 Loop: Biochemical Insights and Implications in Disease.Advances in experimental medicine and biology · 2025Review
- The role of syntaxins in retinal function and health.Frontiers in cellular neuroscience · 2024Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Visual signal transduction takes place within a stack of flattened membranous 'discs' enclosed within the light-sensitive photoreceptor outer segment. The highly curved rims of these discs, formed in the process of disc enclosure, are fortified by large hetero-oligomeric complexes of two homologous tetraspanin proteins, PRPH2 (a.k.a. peripherin-2 or rds) and ROM1. While mutations in PRPH2 affect the formation of disc rims, the role of ROM1 remains poorly understood. In this study, we found that the knockout of ROM1 causes a compensatory increase in the disc content of PRPH2. Despite this increase, discs of ROM1 knockout mice displayed a delay in disc enclosure associated with a large diameter and lack of incisures in mature discs. Strikingly, further increasing the level of PRPH2 rescued these morphological defects. We next showed that disc rims are still formed in a knockin mouse in which the tetraspanin body of PRPH2 was replaced with that of ROM1. Together, these results demonstrate that, despite its contribution to the formation of disc rims, ROM1 can be replaced by an excess of PRPH2 for timely enclosure of newly forming discs and establishing normal outer segment structure.
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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.