ArticleCellular signalling2013
Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding.
Article in Cellular signalling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Lipid nanoparticle technologies for the study of G protein-coupled receptors in lipid environments.Biophysical reviews · 2020Review
- Retinal degeneration in mice expressing the constitutively active G90D rhodopsin mutant.Human molecular genetics · 2020Article
- Article
- Plethora of functions packed into 45 kDa arrestins: biological implications and possible therapeutic strategies.Cellular and molecular life sciences : CMLS · 2019Review
- GPCRs and Signal Transducers: Interaction Stoichiometry.Trends in pharmacological sciences · 2018Review
- Isolation and structure-function characterization of a signaling-active rhodopsin-G protein complex.The Journal of biological chemistry · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Structural role of the T94I rhodopsin mutation in congenital stationary night blindness.EMBO reports · 2016Article
- Hitchhiking on the heptahelical highway: structure and function of 7TM receptor complexes.Nature reviews. Molecular cell biology · 2016Review
- Functional map of arrestin binding to phosphorylated opsin, with and without agonist.Scientific reports · 2016Article
- Article
- The rhodopsin-arrestin-1 interaction in bicelles.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains.Cellular signalling · 2014Article
- Extensive shape shifting underlies functional versatility of arrestins.Current opinion in cell biology · 2014Review
- Functional map of arrestin-1 at single amino acid resolution.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Assembly of an activated rhodopsin-transducin complex in nanoscale lipid bilayers.Biochemistry · 2014Article
- Enhanced phosphorylation-independent arrestins and gene therapy.Handbook of experimental pharmacology · 2014Article
- Constitutively active rhodopsin and retinal disease.Advances in pharmacology (San Diego, Calif.) · 2014Review
- Arrestins in apoptosis.Handbook of experimental pharmacology · 2014Article
- Self-association of arrestin family members.Handbook of experimental pharmacology · 2014Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
The effects of activating mutations associated with night blindness on the stoichiometry of rhodopsin interactions with G protein-coupled receptor kinase 1 (GRK1) and arrestin-1 have not been reported. Here we show that the monomeric form of WT rhodopsin and its constitutively active mutants M257Y, G90D, and T94I, reconstituted into HDL particles are effectively phosphorylated by GRK1, as well as two more ubiquitously expressed subtypes, GRK2 and GRK5. All versions of arrestin-1 tested (WT, pre-activated, and constitutively monomeric mutants) bind to monomeric rhodopsin and show the same selectivity for different functional forms of rhodopsin as in native disc membranes. Rhodopsin phosphorylation by GRK1 and GRK2 promotes arrestin-1 binding to a comparable extent, whereas similar phosphorylation by GRK5 is less effective, suggesting that not all phosphorylation sites on rhodopsin are equivalent in promoting arrestin-1 binding. The binding of WT arrestin-1 to phospho-opsin is comparable to the binding to its preferred target, P-Rh*, suggesting that in photoreceptors arrestin-1 only dissociates after opsin regeneration with 11-cis-retinal, which converts phospho-opsin into inactive phospho-rhodopsin that has lower affinity for arrestin-1. Reduced binding of arrestin-1 to the phospho-opsin form of G90D mutant likely contributes to night blindness caused by this mutation in humans.
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