ArticleThe Journal of biological chemistry2017
Functional role of the three conserved cysteines in the N domain of visual arrestin-1.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- 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
- 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
- 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
- Structural biology of G protein-coupled receptor signaling complexes.Protein science : a publication of the Protein Society · 2019Review
- Arrestin mutations: Some cause diseases, others promise cure.Progress in molecular biology and translational science · 2019Review
- Molecular Defects of the Disease-Causing Human Arrestin-1 C147F Mutant.Investigative ophthalmology & visual science · 2018Article
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Authors and funding
7 authors.
Funding
Abstract
Arrestins specifically bind active and phosphorylated forms of their cognate G protein-coupled receptors, blocking G protein coupling and often redirecting the signaling to alternative pathways. High-affinity receptor binding is accompanied by two major structural changes in arrestin: release of the C-tail and rotation of the two domains relative to each other. The first requires detachment of the arrestin C-tail from the body of the molecule, whereas the second requires disruption of the network of charge-charge interactions at the interdomain interface, termed the polar core. These events can be facilitated by mutations destabilizing the polar core or the anchoring of the C-tail that yield "preactivated" arrestins that bind phosphorylated and unphosphorylated receptors with high affinity. Here we explored the functional role in arrestin activation of the three native cysteines in the N domain, which are conserved in all arrestin subtypes. Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations. Thus, these three conserved cysteines play a role in the domain rotation but not in the C-tail release.
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