ArticleThe Journal of biological chemistry2013
Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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.
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Who cites it
26 citing papers in PubMed, 3 citations in OpenAlex.
- Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024Review
- Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements.International journal of molecular sciences · 2023Article
- Plethora of functions packed into 45 kDa arrestins: biological implications and possible therapeutic strategies.Cellular and molecular life sciences : CMLS · 2019Review
- The structural basis of the arrestin binding to GPCRs.Molecular and cellular endocrinology · 2019Review
- Arrestin-1 engineering facilitates complex stabilization with native rhodopsin.Scientific reports · 2019Article
- Article
- Molecular Defects of the Disease-Causing Human Arrestin-1 C147F Mutant.Investigative ophthalmology & visual science · 2018Article
- Molecular Mechanisms of GPCR Signaling: A Structural Perspective.International journal of molecular sciences · 2017Review
- Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors.Cellular signalling · 2017Article
- Functional role of the three conserved cysteines in the N domain of visual arrestin-1.The Journal of biological chemistry · 2017Article
- A Novel Dominant Mutation in SAG, the Arrestin-1 Gene, Is a Common Cause of Retinitis Pigmentosa in Hispanic Families in the Southwestern United States.Investigative ophthalmology & visual science · 2017Article
- Structural evidence for the role of polar core residue Arg175 in arrestin activation.Scientific reports · 2015Article
- Beyond traditional pharmacology: new tools and approaches.British journal of pharmacology · 2015Review
- Article
- The rhodopsin-arrestin-1 interaction in bicelles.Methods in molecular biology (Clifton, N.J.) · 2015Article
- Identification of receptor binding-induced conformational changes in non-visual arrestins.The Journal of biological chemistry · 2014Article
- Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains.Cellular signalling · 2014Article
- Extensive shape shifting underlies functional versatility of arrestins.Current opinion in cell biology · 2014Review
- Functional map of arrestin-1 at single amino acid resolution.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Therapeutic potential of small molecules and engineered proteins.Handbook of experimental pharmacology · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Arrestin-1 selectively binds active phosphorylated rhodopsin (P-Rh*), demonstrating much lower affinity for inactive phosphorylated (P-Rh) and unphosphorylated active (Rh*) forms. Receptor interaction induces significant conformational changes in arrestin-1, which include large movement of the previously neglected 139-loop in the center of the receptor binding surface, away from the incoming receptor. To elucidate the functional role of this loop, in mouse arrestin-1 we introduced deletions of variable lengths and made several substitutions of Lys-142 in it and Asp-72 in the adjacent loop. Several mutants with perturbations in the 139-loop demonstrate increased binding to P-Rh*, dark P-Rh, Rh*, and phospho-opsin. Enhanced binding of arrestin-1 mutants to non-preferred forms of rhodopsin correlates with decreased thermal stability. The 139-loop perturbations increase P-Rh* binding of arrestin-1 at low temperatures and further change its binding profile on the background of 3A mutant, where the C-tail is detached from the body of the molecule by triple alanine substitution. Thus, the 139-loop stabilizes basal conformation of arrestin-1 and acts as a brake, preventing its binding to non-preferred forms of rhodopsin. Conservation of this loop in other subtypes suggests that it has the same function in all members of the arrestin family.
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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 OpenQuestion graph.