ArticleStructure (London, England : 1993)2022
Structural evidence for visual arrestin priming via complexation of phosphoinositols.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 25 citations in OpenAlex.
- Arrestins as programmable integrators of GPCR signaling: structural microstates, spatiotemporal logic, and therapeutic control.Cell discovery · 2026Review
- Proteome-wide quantification of inositol pyrophosphate-protein interactions.Nature communications · 2026Article
- Deceptive beauty of non-natural structures.Protein science : a publication of the Protein Society · 2026Review
- The Functional Role of Gate Loop Residues in Arrestin Binding to GPCRs.International journal of molecular sciences · 2025Article
- GA-independent DELLA regulation by inositol pyrophosphate in a nonvascular land plant.Nature chemical biology · 2025Article
- Arrestins as Possible Drug Targets.Biomolecules & therapeutics · 2025Review
- Conformational dynamics of the active state of β-arrestin 1.bioRxiv : the preprint server for biology · 2025Article
- Lipids modulate the dynamics of GPCR:β-arrestin interaction.Nature communications · 2025Article
- Structure and self-association of Arrestin-1.Journal of structural biology · 2025Review
- Insights into the Activation and Self-Association of Arrestin-1.Biochemistry · 2025Article
- The Role of Individual Residues in the N-Terminus of Arrestin-1 in Rhodopsin Binding.International journal of molecular sciences · 2025Article
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Expression of Untagged Arrestins in E. coli and Their Purification.Current protocols · 2023Article
- Article
- Stress resilience-enhancing drugs preserve tissue structure and function in degenerating retina via phosphodiesterase inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural view of G protein-coupled receptor signaling in the retinal rod outer segment.Trends in biochemical sciences · 2023Review
- The Role of Arrestin-1 Middle Loop in Rhodopsin Binding.International journal of molecular sciences · 2022Article
- Solo vs. Chorus: Monomers and Oligomers of Arrestin Proteins.International journal of molecular sciences · 2022Review
- Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors.International journal of molecular sciences · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 5 institutions in 4 countries.
Funding
Abstract
Visual arrestin (Arr1) terminates rhodopsin signaling by blocking its interaction with transducin. To do this, Arr1 translocates from the inner to the outer segment of photoreceptors upon light stimulation. Mounting evidence indicates that inositol phosphates (InsPs) affect Arr1 activity, but the Arr1-InsP molecular interaction remains poorly defined. We report the structure of bovine Arr1 in a ligand-free state featuring a near-complete model of the previously unresolved C-tail, which plays a crucial role in regulating Arr1 activity. InsPs bind to the N-domain basic patch thus displacing the C-tail, suggesting that they prime Arr1 for interaction with rhodopsin and help direct Arr1 translocation. These structures exhibit intact polar cores, suggesting that C-tail removal by InsP binding is insufficient to activate Arr1. These results show how Arr1 activity can be controlled by endogenous InsPs in molecular detail.
Indexed as
Identifiers
What Socratic 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 Socratic graph.