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Tóth, András D; Gyombolai, Pál; Szalai, Bence; Várnai, Péter; Turu, Gábor; Hunyady, László
Molecular and cellular endocrinology, 02/2017, Letnik: 442Journal Article
Heterodimerization between angiotensin type 1A receptor (AT R) and β -adrenergic receptor (β AR) has been shown to modulate G protein-mediated effects of these receptors. Activation of G protein-coupled receptors (GPCRs) leads to β-arrestin binding, desensitization, internalization and G protein-independent signaling of GPCRs. Our aim was to study the effect of heterodimerization on β-arrestin coupling. We found that β-arrestin binding of β AR is affected by activation of AT Rs. Costimulation with angiotensin II and isoproterenol markedly enhanced the interaction between β AR and β-arrestins, by prolonging the lifespan of β AR-induced β-arrestin2 clusters at the plasma membrane. While candesartan, a conventional AT R antagonist, had no effect on the β-arrestin2 binding to β AR, TRV120023, a β-arrestin biased agonist, enhanced the interaction. These findings reveal a new crosstalk mechanism between AT R and β AR, and suggest that enhanced β-arrestin2 binding to β AR can contribute to the pharmacological effects of biased AT R agonists.
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