ArticleThe Journal of general physiology1999
Occupancy of the chromophore binding site of opsin activates visual transduction in rod photoreceptors.
Article in The Journal of general physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- The physiology of dark adaptation: Progress and future directions.Progress in retinal and eye research · 2025Review
- Opsin 3-GAmerican journal of respiratory cell and molecular biology · 2021Article
- Light-Mediated Inhibition of Colonic Smooth Muscle Constriction and Colonic MotilityFrontiers in physiology · 2021Article
- Novel fluorescent GPCR biosensor detects retinal equilibrium binding to opsin and active G protein and arrestin signaling conformations.The Journal of biological chemistry · 2020Article
- Apo-Opsin Exists in Equilibrium Between a Predominant Inactive and a Rare Highly Active State.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- cis Retinol oxidation regulates photoreceptor access to the retina visual cycle and cone pigment regeneration.The Journal of physiology · 2016Article
- The role of the non-covalent β-ionone-ring binding site in rhodopsin: historical and physiological perspective.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2015Article
- New insights into retinoid metabolism and cycling within the retina.Progress in retinal and eye research · 2013Review
- Mislocalized opsin and cAMP signaling: a mechanism for sprouting by rod cells in retinal degeneration.Investigative ophthalmology & visual science · 2012Article
- The role of the lipid matrix for structure and function of the GPCR rhodopsin.Biochimica et biophysica acta · 2012Review
- Rod and cone visual pigments and phototransduction through pharmacological, genetic, and physiological approaches.The Journal of biological chemistry · 2012Review
- Vitamin A activates rhodopsin and sensitizes it to ultraviolet light.Visual neuroscience · 2011Article
- Probing human red cone opsin activity with retinal analogues.Journal of natural products · 2011Article
- Binding of more than one retinoid to visual opsins.Biophysical journal · 2010Article
- Assays for inverse agonists in the visual system.Methods in enzymology · 2010Article
- Physiological studies of the interaction between opsin and chromophore in rod and cone visual pigments.Methods in molecular biology (Clifton, N.J.) · 2010Article
- The 9-methyl group of retinal is essential for rapid Meta II decay and phototransduction quenching in red cones.The Journal of general physiology · 2009Article
- Turning cones off: the role of the 9-methyl group of retinal in red cones.The Journal of general physiology · 2006Article
- Cyclic nucleotide-gated ion channels in rod photoreceptors are protected from retinoid inhibition.The Journal of general physiology · 2006Article
- Defining the retinoid binding site in the rod cyclic nucleotide-gated channel.The Journal of general physiology · 2005Article
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Authors and funding
3 authors.
Funding
Abstract
The retinal analogue beta-ionone was used to investigate possible physiological effects of the noncovalent interaction between rod opsin and its chromophore 11-cis retinal. Isolated salamander rod photoreceptors were exposed to bright light that bleached a significant fraction of their pigment, were allowed to recover to a steady state, and then were exposed to beta-ionone. Our experiments show that in bleach-adapted rods beta-ionone causes a decrease in light sensitivity and dark current and an acceleration of the dim flash photoresponse and the rate constants of guanylyl cyclase and cGMP phosphodiesterase. Together, these observations indicate that in bleach-adapted rods beta-ionone activates phototransduction in the dark. Control experiments showed no effect of beta-ionone in either fully dark-adapted or background light-adapted cells, indicating direct interaction of beta-ionone with the free opsin produced by bleaching. We speculate that beta-ionone binds specifically in the chromophore pocket of opsin to produce a complex that is more catalytically potent than free opsin alone. We hypothesize that a similar reaction may occur in the intact retina during pigment regeneration. We propose a model of rod pigment regeneration in which binding of 11-cis retinal to opsin leads to activation of the complex accompanied by a decrease in light sensitivity. The subsequent covalent attachment of retinal to opsin completely inactivates opsin and leads to the recovery of sensitivity. Our findings resolve the conflict between biochemical and physiological data concerning the effect of the occupancy of the chromophore binding site on the catalytic potency of opsin. We show that binding of beta-ionone to rod opsin produces effects opposite to its previously described effects on cone opsin. We propose that this distinction is due to a fundamental difference in the interaction of rod and cone opsins with retinal, which may have implications for the different physiology of the two types of photoreceptors.
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