ArticleThe Journal of biological chemistry2013
Divergent β-arrestin-dependent signaling events are dependent upon sequences within G-protein-coupled receptor C termini.
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 14 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.
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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
14 citing papers in PubMed, 22 citations in OpenAlex.
- Revealing GRK5 Activation Features by Interpretable Machine Learning and Molecular Dynamics Simulation.International journal of molecular sciences · 2026Article
- Association of Neurokinin-1 Receptor Signaling Pathways with Cancer.Current medicinal chemistry · 2024Review
- LPA1-mediated inhibition of CXCR4 attenuates CXCL12-induced signaling and cell migration.Cell communication and signaling : CCS · 2023Article
- Neurokinin-1 receptor promotes non-small cell lung cancer progression through transactivation of EGFR.Cell death & disease · 2022Article
- Quantifying the Kinetics of Signaling and Arrestin Recruitment by Nervous System G-Protein Coupled Receptors.Frontiers in cellular neuroscience · 2021Article
- Smoothened determines β-arrestin-mediated removal of the G protein-coupled receptor Gpr161 from the primary cilium.The Journal of cell biology · 2016Article
- Distinct phosphorylation sites on the ghrelin receptor, GHSR1a, establish a code that determines the functions of ß-arrestins.Scientific reports · 2016Article
- Minireview: Spatial Programming of G Protein-Coupled Receptor Activity: Decoding Signaling in Health and Disease.Molecular endocrinology (Baltimore, Md.) · 2015Review
- Substance P Weights Striatal Dopamine Transmission Differently within the Striosome-Matrix Axis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Engineered hyperphosphorylation of the β2-adrenoceptor prolongs arrestin-3 binding and induces arrestin internalization.Molecular pharmacology · 2015Article
- Article
- Molecular determinants of orexin receptor-arrestin-ubiquitin complex formation.British journal of pharmacology · 2014Article
- β-Arrestin-dependent deactivation of mouse melanopsin.PloS one · 2014Article
- Tachykinins and their receptors: contributions to physiological control and the mechanisms of disease.Physiological reviews · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
β-Arrestins are multifunctional adaptor proteins that, upon recruitment to an activated G-protein-coupled receptor, can promote desensitization of G-protein signaling and receptor internalization while simultaneously eliciting an independent signal. The result of β-arrestin signaling depends upon the activating receptor. For example, activation of two Gα(q)-coupled receptors, protease-activated receptor-2 (PAR(2)) and neurokinin-1 receptor (NK1R), results in drastically different signaling events. PAR(2) promotes β-arrestin-dependent membrane-sequestered extracellular signal-regulated kinase (ERK1/2) activation, cofilin activation, and cell migration, whereas NK1R promotes nuclear ERK1/2 activation and proliferation. Using bioluminescence resonance energy transfer to monitor receptor/β-arrestin interactions in real time, we observe that PAR(2) has a higher apparent affinity for both β-arrestins than does NK1R, recruits them at a faster rate, and exhibits more rapid desensitization of the G-protein signal. Furthermore, recruitment of β-arrestins to PAR(2) does not require prior Gα(q) signaling events, whereas inhibition of Gα(q) signaling intermediates inhibits recruitment of β-arrestins to NK1R. Using chimeric receptors in which the C terminus of PAR(2) is fused to the N terminus of NK1R and vice versa and a critical Ser/Thr mutant of PAR(2), we demonstrate that interactions between β-arrestins and specific phosphoresidues in the C termini of each receptor are crucial for determining the rate and magnitude of β-arrestin recruitment as well as the ultimate signaling outcome.
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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.