ReviewProgress in molecular biology and translational science2013
Structural determinants of arrestin functions.
Review in Progress in molecular biology and translational science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 69 citations in OpenAlex.
- Direct β-arrestin engagement by the non-canonical WNT receptor FZD6 via a shallow binding pocket.Acta pharmacologica Sinica · 2026Article
- Cryo-electron microscopy for GPCR research and drug discovery in endocrinology and metabolism.Nature reviews. Endocrinology · 2024Review
- Surveying nonvisual arrestins reveals allosteric interactions between functional sites.Proteins · 2023Article
- Phosphoproteomic mapping of CCR5 and ACKR2 signaling properties.Frontiers in molecular biosciences · 2022Article
- Article
- Many faces of the GPCR-arrestin interaction.Archives of pharmacal research · 2020Review
- A complex structure of arrestin-2 bound to a G protein-coupled receptor.Cell research · 2019Article
- Review
- The role of GPCRs in bone diseases and dysfunctions.Bone research · 2019Review
- β-arrestin2 functions as a key regulator in the sympathetic-triggered immunodepression after stroke.Journal of neuroinflammation · 2018Article
- Overexpression of ß-Arrestin1 in the Rostral Ventrolateral Medulla Downregulates Angiotensin Receptor and Lowers Blood Pressure in Hypertension.Frontiers in physiology · 2018Article
- Structure and dynamics of GPCR signaling complexes.Nature structural & molecular biology · 2018Review
- A synthetic intrabody-based selective and generic inhibitor of GPCR endocytosis.Nature nanotechnology · 2017Article
- Functional antagonism of β-arrestin isoforms balance IGF-1R expression and signalling with distinct cancer-related biological outcomes.Oncogene · 2017Article
- Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors.Cell · 2017Article
- Arrestin-2 and arrestin-3 differentially modulate locomotor responses and sensitization to amphetamine.Neuropharmacology · 2017Article
- The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling.Pharmacological reviews · 2017Review
- Core engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation.Molecular biology of the cell · 2017Article
- A Comprehensive View of the β-Arrestinome.Frontiers in endocrinology · 2017Article
- Functional competence of a partially engaged GPCR-β-arrestin complex.Nature communications · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Arrestins are a small protein family with only four members in mammals. Arrestins demonstrate an amazing versatility, interacting with hundreds of different G protein-coupled receptor (GPCR) subtypes, numerous nonreceptor signaling proteins, and components of the internalization machinery, as well as cytoskeletal elements, including regular microtubules and centrosomes. Here, we focus on the structural determinants that mediate various arrestin functions. The receptor-binding elements in arrestins were mapped fairly comprehensively, which set the stage for the construction of mutants targeting particular GPCRs. The elements engaged by other binding partners are only now being elucidated and in most cases we have more questions than answers. Interestingly, even very limited and imprecise identification of structural requirements for the interaction with very few other proteins has enabled the development of signaling-biased arrestin mutants. More comprehensive understanding of the structural underpinning of different arrestin functions will pave the way for the construction of arrestins that can link the receptor we want to the signaling pathway of our choosing.
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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.