ArticleNature communications2024
Active state structures of a bistable visual opsin bound to G proteins.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Rhobot-Screen: an integrated robotic platform for functional screening of rhodopsin variants.BMC biology · 2026Article
- Genomic and regulatory basis of visual opsin genes in the cleaner wrasse behavior: features, expression, and enhancer mechanisms.Molecular biology reports · 2026Article
- 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
- Tool antibody fragments reveal multiple conformations of the rhodopsin-Gi signaling complex.Biophysical journal · 2026Article
- A multiscale screening platform for rapid GPCR variant profiling reveals color-tuned JSR1 mutants.Biophysical journal · 2026Article
- Mapping signal transduction in bistable jumping spider rhodopsin 1.Biophysical journal · 2026Article
- The visual system of a nocturnal long-distance migrant, the Australian Bogong moth.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2026Article
- Dragonfly red opsins share a common tuning mechanism with mammalian red opsins and further enhancement of near-infrared sensitivity.Cellular and molecular life sciences : CMLS · 2026Article
- Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Retinoid dynamics in vision: from visual cycle biology to retina disease treatments.Pharmacology & therapeutics · 2025Review
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Authors and funding
12 authors.
Funding
Abstract
Opsins are G protein-coupled receptors (GPCRs) that have evolved to detect light stimuli and initiate intracellular signaling cascades. Their role as signal transducers is critical to light perception across the animal kingdom. Opsins covalently bind to the chromophore 11-cis retinal, which isomerizes to the all-trans isomer upon photon absorption, causing conformational changes that result in receptor activation. Monostable opsins, responsible for vision in vertebrates, release the chromophore after activation and must bind another retinal molecule to remain functional. In contrast, bistable opsins, responsible for non-visual light perception in vertebrates and for vision in invertebrates, absorb a second photon in the active state to return the chromophore and protein to the inactive state. Structures of bistable opsins in the activated state have proven elusive, limiting our understanding of how they function as bidirectional photoswitches. Here we present active state structures of a bistable opsin, jumping spider rhodopsin isoform-1 (JSR1), in complex with its downstream signaling partners, the G
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