ArticleScientific reports2015
Structural evidence for the role of polar core residue Arg175 in arrestin activation.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Deceptive beauty of non-natural structures.Protein science : a publication of the Protein Society · 2026Review
- Structure and self-association of Arrestin-1.Journal of structural biology · 2025Review
- Insights into the Activation and Self-Association of Arrestin-1.Biochemistry · 2025Article
- Article
- GPCR binding and JNK3 activation by arrestin-3 have different structural requirements.bioRxiv : the preprint server for biology · 2023Article
- G protein-coupled receptor signaling: transducers and effectors.American journal of physiology. Cell physiology · 2022Review
- Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Receptor-Arrestin Interactions: The GPCR Perspective.Biomolecules · 2021Review
- Many faces of the GPCR-arrestin interaction.Archives of pharmacal research · 2020Review
- Crystal Structure of β-Arrestin 2 in Complex with CXCR7 Phosphopeptide.Structure (London, England : 1993) · 2020Article
- Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin.Scientific reports · 2020Article
- The single nucleotide β -arrestin2 variant, A248T, resembles dynamical properties of activated arrestin.Turkish journal of chemistry · 2020Article
- Arrestins: structural disorder creates rich functionality.Protein & cell · 2018Review
- Structural Basis of Arrestin-Dependent Signal Transduction.Trends in biochemical sciences · 2018Review
- Structure and dynamics of GPCR signaling complexes.Nature structural & molecular biology · 2018Review
- Structural basis of arrestin-3 activation and signaling.Nature communications · 2017Article
- Functional role of the three conserved cysteines in the N domain of visual arrestin-1.The Journal of biological chemistry · 2017Article
- C-edge loops of arrestin function as a membrane anchor.Nature communications · 2017Article
- Functional map of arrestin binding to phosphorylated opsin, with and without agonist.Scientific reports · 2016Article
- The β-Arrestins: Multifunctional Regulators of G Protein-coupled Receptors.The Journal of biological chemistry · 2016Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Binding mechanism of arrestin requires photoactivation and phosphorylation of the receptor protein rhodopsin, where the receptor bound phosphate groups cause displacement of the long C-tail 'activating' arrestin. Mutation of arginine 175 to glutamic acid (R175E), a central residue in the polar core and previously predicted as the 'phosphosensor' leads to a pre-active arrestin that is able to terminate phototransduction by binding to non-phosphorylated, light-activated rhodopsin. Here, we report the first crystal structure of a R175E mutant arrestin at 2.7 Å resolution that reveals significant differences compared to the basal state reported in full-length arrestin structures. These differences comprise disruption of hydrogen bond network in the polar core, and three-element interaction including disordering of several residues in the receptor-binding finger loop and the C-terminus (residues 361-404). Additionally, R175E structure shows a 7.5° rotation of the amino and carboxy-terminal domains relative to each other. Consistent to the biochemical data, our structure suggests an important role of R29 in the initial activation step of C-tail release. Comparison of the crystal structures of basal arrestin and R175E mutant provide insights into the mechanism of arrestin activation, where binding of the receptor likely induces structural changes mimicked as in R175E.
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