ArticleProceedings of the National Academy of Sciences of the United States of America2017
Dephosphorylation by protein phosphatase 2A regulates visual pigment regeneration and the dark adaptation of mammalian photoreceptors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- The physiology of dark adaptation: Progress and future directions.Progress in retinal and eye research · 2025Review
- Structure and self-association of Arrestin-1.Journal of structural biology · 2025Review
- C. elegans PPEF-type phosphatase (Retinal degeneration C ortholog) functions in diverse classes of cilia to regulate nematode behaviors.Scientific reports · 2024Article
- Investigating the Role of RhodopsineNeuro · 2023Article
- Deletion of Protein Phosphatase 2A Accelerates Retinal Degeneration in GRK1- and Arr1-Deficient Mice.Investigative ophthalmology & visual science · 2022Article
- Arrestin Facilitates Rhodopsin DephosphorylationThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Retinal pigment epithelium-specific CLIC4 mutant is a mouse model of dry age-related macular degeneration.Nature communications · 2022Article
- Renal ATCirculation research · 2022Article
- Shedding light on dark adaptation.The biochemist · 2020Article
- Protein Phosphatase 2A and Clathrin-Mediated Endocytosis Facilitate Robust Melanopsin Light Responses and Resensitization.Investigative ophthalmology & visual science · 2020Article
- Phosphorylation at Serine 21 in G protein-coupled receptor kinase 1 (GRK1) is required for normal kinetics of dark adaption in rod but not cone photoreceptors.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- A non-retinoid antagonist of retinol-binding protein 4 rescues phenotype in a model of Stargardt disease without inhibiting the visual cycle.The Journal of biological chemistry · 2018Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Resetting of G-protein-coupled receptors (GPCRs) from their active state back to their biologically inert ground state is an integral part of GPCR signaling. This "on-off" GPCR cycle is regulated by reversible phosphorylation. Retinal rod and cone photoreceptors arguably represent the best-understood example of such GPCR signaling. Their visual pigments (opsins) are activated by light, transduce the signal, and are then inactivated by a GPCR kinase and arrestin. Although pigment inactivation by phosphorylation is well understood, the enzyme(s) responsible for pigment dephosphorylation and the functional significance of this reaction remain unknown. Here, we show that protein phosphatase 2A (PP2A) acts as opsin phosphatase in both rods and cones. Elimination of PP2A substantially slows pigment dephosphorylation, visual chromophore recycling, and ultimately photoreceptor dark adaptation. These findings demonstrate that visual pigment dephosphorylation regulates the dark adaptation of photoreceptors and provide insights into the role of this reaction in GPCR signaling.
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