ArticleProceedings of the National Academy of Sciences of the United States of America2016
Dimerization of visual pigments in vivo.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- Multiple opsin expression in cubozoan ocelli indicates functional redundancy.Scientific reports · 2026Article
- Photoreceptor-targeted extracellular vesicles-mediated delivery of Cul7 siRNA for retinal degeneration therapy.Theranostics · 2024Article
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- The MProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Expression of Opsins of the Box JellyfishFrontiers in neuroanatomy · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021Review
- Functional compartmentalization of photoreceptor neurons.Pflugers Archiv : European journal of physiology · 2021Review
- Evolutionary Constraint on Visual and Nonvisual Mammalian Opsins.Journal of biological rhythms · 2021Article
- Compartmentalization of Photoreceptor Sensory Cilia.Frontiers in cell and developmental biology · 2021Review
- The F220C and F45L rhodopsin mutations identified in retinitis pigmentosa patients do not cause pathology in mice.Scientific reports · 2020Article
- Cryo-EM structure of the native rhodopsin dimer in nanodiscs.The Journal of biological chemistry · 2019Article
- Stereospecific modulation of dimeric rhodopsin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Human nonvisual opsin 3 regulates pigmentation of epidermal melanocytes through functional interaction with melanocortin 1 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Disruption of Rhodopsin Dimerization in Mouse Rod Photoreceptors by Synthetic Peptides Targeting Dimer Interface.Methods in molecular biology (Clifton, N.J.) · 2018Article
- A G Protein-Coupled Receptor Dimerization Interface in Human Cone Opsins.Biochemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 4 institutions in 1 country.
Funding
Abstract
It is a deeply engrained notion that the visual pigment rhodopsin signals light as a monomer, even though many G protein-coupled receptors are now known to exist and function as dimers. Nonetheless, recent studies (albeit all in vitro) have suggested that rhodopsin and its chromophore-free apoprotein, R-opsin, may indeed exist as a homodimer in rod disk membranes. Given the overwhelmingly strong historical context, the crucial remaining question, therefore, is whether pigment dimerization truly exists naturally and what function this dimerization may serve. We addressed this question in vivo with a unique mouse line (S-opsin(+)Lrat(-/-)) expressing, transgenically, short-wavelength-sensitive cone opsin (S-opsin) in rods and also lacking chromophore to exploit the fact that cone opsins, but not R-opsin, require chromophore for proper folding and trafficking to the photoreceptor's outer segment. In R-opsin's absence, S-opsin in these transgenic rods without chromophore was mislocalized; in R-opsin's presence, however, S-opsin trafficked normally to the rod outer segment and produced functional S-pigment upon subsequent chromophore restoration. Introducing a competing R-opsin transmembrane helix H1 or helix H8 peptide, but not helix H4 or helix H5 peptide, into these transgenic rods caused mislocalization of R-opsin and S-opsin to the perinuclear endoplasmic reticulum. Importantly, a similar peptide-competition effect was observed even in WT rods. Our work provides convincing evidence for visual pigment dimerization in vivo under physiological conditions and for its role in pigment maturation and targeting. Our work raises new questions regarding a potential mechanistic role of dimerization in rhodopsin signaling.
Indexed as
Identifiers
What OpenQuestion holds
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.