ArticleJournal of cell science2022
Divergent G-protein selectivity across melanopsins from mice and humans.
Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- A Pentaradial and Bilateral Combined Photoreception System in the Sea Cucumber is Mediated by a Blue Light-Sensitive R-Opsin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Kinetic model of partial agonism reveals cellular basis of ligand efficacy.The Journal of biological chemistry · 2026Article
- RGS proteins: Potential regulators of mouse melanopsin's signaling phototransduction cascade across ipRGC subtypes.Biophysical journal · 2026Article
- Development of visible light-sensitive human neuropsin (OPN5) via single amino acid substitution.FEBS letters · 2025Article
- Molecular basis underlying the specificity of an antagonist AA92593 for mammalian melanopsins.The Journal of biological chemistry · 2025Article
- In-silico predicted mouse melanopsins with blue spectral shifts deliver efficient subcellular signaling.Cell communication and signaling : CCS · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Melanopsin is an opsin photopigment and light-activated G-protein-coupled receptor; it is expressed in photoreceptive retinal ganglion cells (mRGCs) and can be employed as an optogenetic tool. Mammalian melanopsins can signal via Gq/11 and Gi/o/t heterotrimeric G proteins, but aspects of the mRGC light response appear incompatible with either mode of signalling. We use live-cell reporter assays in HEK293T cells to show that melanopsins from mice and humans can also signal via Gs. We subsequently show that this mode of signalling is substantially divergent between species. The two established structural isoforms of mouse melanopsin (which differ in the length of their C-terminal tail) both signalled strongly through all three G-protein classes (Gq/11, Gi/o and Gs), whereas human melanopsin showed weaker signalling through Gs. Our data identify Gs as a new mode of signalling for mammalian melanopsins and reveal diversity in G-protein selectivity across mammalian melanopsins.
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Registered trials
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