ArticleProceedings of the National Academy of Sciences of the United States of America2013
Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 109 citations in OpenAlex.
- Deceptive beauty of non-natural structures.Protein science : a publication of the Protein Society · 2026Review
- Distinct membrane binding properties of the two non-visual arrestins.Communications biology · 2026Article
- The physiology of dark adaptation: Progress and future directions.Progress in retinal and eye research · 2025Review
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Illuminating GPCR signaling mechanisms by NMR spectroscopy with stable-isotope labeled receptors.Current opinion in pharmacology · 2023Review
- Review
- Expression of Untagged Arrestins in E. coli and Their Purification.Current protocols · 2023Article
- Conformational flexibility underlies the versatility of arrestins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- ACKR3-arrestin2/3 complexes reveal molecular consequences of GRK-dependent barcoding.bioRxiv : the preprint server for biology · 2023Article
- Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements.International journal of molecular sciences · 2023Article
- The Role of Arrestin-1 Middle Loop in Rhodopsin Binding.International journal of molecular sciences · 2022Article
- β-arrestin1 promotes tauopathy by transducing GPCR signaling, disrupting microtubules and autophagy.Life science alliance · 2022Article
- Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR.Nature communications · 2021Article
- Functional compartmentalization of photoreceptor neurons.Pflugers Archiv : European journal of physiology · 2021Review
- Signaling-Biased and Constitutively Active Dopamine D2 Receptor Variant.ACS chemical neuroscience · 2021Article
- An Eight Amino Acid Segment Controls Oligomerization and Preferred Conformation of the two Non-visual Arrestins.Journal of molecular biology · 2021Article
- Receptor-Arrestin Interactions: The GPCR Perspective.Biomolecules · 2021Review
- Biological Role of Arrestin-1 Oligomerization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin.Scientific reports · 2020Article
- Biased GPCR signaling: Possible mechanisms and inherent limitations.Pharmacology & therapeutics · 2020Review
17 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Solution NMR spectroscopy of labeled arrestin-1 was used to explore its interactions with dark-state phosphorylated rhodopsin (P-Rh), phosphorylated opsin (P-opsin), unphosphorylated light-activated rhodopsin (Rh*), and phosphorylated light-activated rhodopsin (P-Rh*). Distinct sets of arrestin-1 elements were seen to be engaged by Rh* and inactive P-Rh, which induced conformational changes that differed from those triggered by binding of P-Rh*. Although arrestin-1 affinity for Rh* was seen to be low (K(D) > 150 μM), its affinity for P-Rh (K(D) ~80 μM) was comparable to the concentration of active monomeric arrestin-1 in the outer segment, suggesting that P-Rh generated by high-gain phosphorylation is occupied by arrestin-1 under physiological conditions and will not signal upon photo-activation. Arrestin-1 was seen to bind P-Rh* and P-opsin with fairly high affinity (K(D) of~50 and 800 nM, respectively), implying that arrestin-1 dissociation is triggered only upon P-opsin regeneration with 11-cis-retinal, precluding noise generated by opsin activity. Based on their observed affinity for arrestin-1, P-opsin and inactive P-Rh very likely affect the physiological monomer-dimer-tetramer equilibrium of arrestin-1, and should therefore be taken into account when modeling photoreceptor function. The data also suggested that complex formation with either P-Rh* or P-opsin results in a global transition in the conformation of arrestin-1, possibly to a dynamic molten globule-like structure. We hypothesize that this transition contributes to the mechanism that triggers preferential interactions of several signaling proteins with receptor-activated arrestins.
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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.