ArticleNature communications2012
Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin.
Article in Nature communications, 2012. 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 45 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed, 81 citations in OpenAlex.
- A key amino acid site associated with rhodopsin mammal evolution to diurnal vision.Scientific reports · 2025Article
- Small angle neutron scattering study of rhodopsin oligomerization and G-protein coupling in a physiologically relevant lipid membrane.Biochimica et biophysica acta. Biomembranes · 2025Review
- Bidirectional Phosphorylation Changes in Opsins Associated With Early Myopia and Hyperopia Signal Regulation by Phosphoproteomics.Investigative ophthalmology & visual science · 2025Article
- Lipids modulate the dynamics of GPCR:β-arrestin interaction.Nature communications · 2025Article
- A rapid, tag-free way to purify functional GPCRs.The Journal of biological chemistry · 2024Article
- Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor.Nature communications · 2022Article
- Ancient whale rhodopsin reconstructs dim-light vision over a major evolutionary transition: Implications for ancestral diving behavior.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors.International journal of molecular sciences · 2021Review
- Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021Review
- Article
- Novel fluorescent GPCR biosensor detects retinal equilibrium binding to opsin and active G protein and arrestin signaling conformations.The Journal of biological chemistry · 2020Article
- Article
- A complex structure of arrestin-2 bound to a G protein-coupled receptor.Cell research · 2019Article
- Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation.Nature communications · 2019Article
- Article
- Article
- Structure and dynamics of GPCR signaling complexes.Nature structural & molecular biology · 2018Review
- C-edge loops of arrestin function as a membrane anchor.Nature communications · 2017Article
- Functional competence of a partially engaged GPCR-β-arrestin complex.Nature communications · 2016Article
- Quaternary structures of opsin in live cells revealed by FRET spectrometry.The Biochemical journal · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-protein-coupled receptors are universally regulated by arrestin binding. Here we show that rod arrestin induces uptake of the agonist all-trans-retinal [corrected] in only half the population of phosphorylated opsin in the native membrane. Agonist uptake blocks subsequent entry of the inverse agonist 11-cis-retinal (that is, regeneration of rhodopsin), but regeneration is not blocked in the other half of aporeceptors. Environmentally sensitive fluorophores attached to arrestin reported that conformational changes in loop(V-VI) (N-domain) are coupled to the entry of agonist, while loop(XVIII-XIX) (C-domain) engages the aporeceptor even before agonist is added. The data are most consistent with a model in which each domain of arrestin engages its own aporeceptor, and the different binding preferences of the domains lead to asymmetric ligand binding by the aporeceptors. Such a mechanism would protect the rod cell in bright light by concurrently sequestering toxic all-trans-retinal [corrected] and allowing regeneration with 11-cis-retinal.
Indexed as
Identifiers
What OpenQuestion holds
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.