ArticleJournal of neurochemistry2021
The finger loop as an activation sensor in arrestin.
Article in Journal of neurochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Phosphorylation site topology governs the functional dynamics of arrestin recruitment to GPCRs.Research square · 2026Article
- Article
- 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
- The role of arrestin-1 N-edge in rhodopsin binding.Cellular signalling · 2025Article
- IgStrand: A universal residue numbering scheme for the immunoglobulin-fold (Ig-fold) to study Ig-proteomes and Ig-interactomes.PLoS computational biology · 2025Review
- The Role of Individual Residues in the N-Terminus of Arrestin-1 in Rhodopsin Binding.International journal of molecular sciences · 2025Article
- Ig or Not Ig? That Is the Question: The Nucleating Supersecondary Structure of the Ig-Fold and the Extended Ig Universe.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Article
- Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements.International journal of molecular sciences · 2023Article
- GPCR binding and JNK3 activation by arrestin-3 have different structural requirements.bioRxiv : the preprint server for biology · 2023Article
- The Role of Arrestin-1 Middle Loop in Rhodopsin Binding.International journal of molecular sciences · 2022Article
- Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors.International journal of molecular sciences · 2021Review
- Receptor-Arrestin Interactions: The GPCR Perspective.Biomolecules · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The finger loop in the central crest of the receptor-binding site of arrestins engages the cavity between the transmembrane helices of activated G-protein-coupled receptors. Therefore, it was hypothesized to serve as the sensor that detects the activation state of the receptor. We performed comprehensive mutagenesis of the finger loop in bovine visual arrestin-1, generated mutant radiolabeled proteins by cell-free translation, and determined the effects of mutations on the in vitro binding of arrestin-1 to purified phosphorylated light-activated rhodopsin. This interaction is driven by two factors, rhodopsin activation and rhodopsin-attached phosphates. Therefore, the binding of arrestin-1 to light-activated unphosphorylated rhodopsin is low. To evaluate the role of the finger loop specifically in the recognition of the active receptor conformation, we tested the effects of these mutations in the context of truncated arrestin-1 that demonstrates much higher binding to unphosphorylated activated and phosphorylated inactive rhodopsin. The majority of finger loop residues proved important for arrestin-1 binding to light-activated rhodopsin, with six mutations affecting the binding exclusively to this form. Thus, the finger loop is the key element of arrestin-1 activation sensor. The data also suggest that arrestin-1 and its enhanced mutant bind various functional forms of rhodopsin differently.
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