Regulation of G Protein-Coupled Receptors by Receptor Kinases and Arrestins
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2022, Biochemical PharmacologyCitation Excerpt :Several reports have indicated that GPCRs are phosphorylated in a unique manner. The initial findings suggest that GPCR phosphorylation by specific kinases is required for the dissociation of the receptor from the coupled G-proteins, followed by the recruitment of arrestins to terminate the signaling [125–128]. The receptor-arrestin complex associates with various proteins involved in the formation of clathrin-coated pits, leading to receptor internalization [127,129].
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2014, From Molecules to Networks: An Introduction to Cellular and Molecular Neuroscience: Third EditionThe chemokine receptor CCR1 is constitutively active, which leads to G protein-independent, β-arrestin-mediated internalization
2013, Journal of Biological ChemistryCitation Excerpt :Agonist binding to GPCRs typically results in G protein activation followed by receptor desensitization mediated by phosphorylation of intracellular domains and recruitment of arrestins. The arrestin proteins sterically occlude the receptor from further G protein coupling and connect the receptor to the internalization machinery of the cell to initiate endocytosis (54). Here it was tested whether CCR1 is internalized in the absence of agonist in various cell systems.
Antinociceptive potentiation and attenuation of tolerance by intrathecal β-arrestin 2 small interfering RNA in rats
2011, British Journal of AnaesthesiaCitation Excerpt :In addition, β-arrestin has been demonstrated as playing an important role in regulating opioid receptors.7 8 β-arrestins, including β-arrestin 1 and β-arrestin 2, are predominantly expressed in neuronal tissues (low expression can be detected in most tissues)9 and regulate G-protein-coupled receptor coupling and signalling.10 In β-arrestin 2 knockout mice, the tolerance to the antinociceptive effects was significantly attenuated in the tail-flick (TF) test.8 11
Intact cell binding for in vitro prediction of sedative and non-sedative histamine H<inf>1</inf>-receptor antagonists based on receptor internalization
2008, Journal of Pharmacological SciencesN-terminal tyrosine modulation of the endocytic adaptor function of the β-arrestins
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