ArticleScientific reports2016
Functional map of arrestin binding to phosphorylated opsin, with and without agonist.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- The Functional Role of Gate Loop Residues in Arrestin Binding to GPCRs.International journal of molecular sciences · 2025Article
- The role of arrestin-1 N-edge in rhodopsin binding.Cellular signalling · 2025Article
- The Role of Individual Residues in the N-Terminus of Arrestin-1 in Rhodopsin Binding.International journal of molecular sciences · 2025Article
- Exploring the therapeutic potential of sγPNA-141: Pharmacodynamics and mechanistic insights during ischemic stroke recovery.Molecular therapy. Nucleic acids · 2024Article
- Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements.International journal of molecular sciences · 2023Article
- β-arrestin1 and 2 exhibit distinct phosphorylation-dependent conformations when coupling to the same GPCR in living cells.Nature communications · 2022Article
- Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors.International journal of molecular sciences · 2021Review
- The finger loop as an activation sensor in arrestin.Journal of neurochemistry · 2021Article
- Lysine in the lariat loop of arrestins does not serve as phosphate sensor.Journal of neurochemistry · 2021Article
- Article
- Biological Role of Arrestin-1 Oligomerization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Article
- Plethora of functions packed into 45 kDa arrestins: biological implications and possible therapeutic strategies.Cellular and molecular life sciences : CMLS · 2019Review
- Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation.Nature communications · 2019Article
- Arrestin-1 engineering facilitates complex stabilization with native rhodopsin.Scientific reports · 2019Article
- Article
- Structural Basis of Arrestin-Dependent Signal Transduction.Trends in biochemical sciences · 2018Review
- Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation.Nature structural & molecular biology · 2018Article
- Structure and dynamics of GPCR signaling complexes.Nature structural & molecular biology · 2018Review
- Arrestins: Introducing Signaling Bias Into Multifunctional Proteins.Progress in molecular biology and translational science · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arrestins desensitize G protein-coupled receptors (GPCRs) and act as mediators of signalling. Here we investigated the interactions of arrestin-1 with two functionally distinct forms of the dim-light photoreceptor rhodopsin. Using unbiased scanning mutagenesis we probed the individual contribution of each arrestin residue to the interaction with the phosphorylated apo-receptor (Ops-P) and the agonist-bound form (Meta II-P). Disruption of the polar core or displacement of the C-tail strengthened binding to both receptor forms. In contrast, mutations of phosphate-binding residues (phosphosensors) suggest the phosphorylated receptor C-terminus binds arrestin differently for Meta II-P and Ops-P. Likewise, mutations within the inter-domain interface, variations in the receptor-binding loops and the C-edge of arrestin reveal different binding modes. In summary, our results indicate that arrestin-1 binding to Meta II-P and Ops-P is similarly dependent on arrestin activation, although the complexes formed with these two receptor forms are structurally distinct.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.