Abstract
Agonist-triggered downregulation of β-adrenergic receptors (ARs) constitutes vital negative feedback to prevent cellular overexcitation. Patriarchi et al (EMBO J 2016;35:1330, PMID 27103070) report a novel downregulation of β2AR signaling highly specific for Cav1.2. They find that β2AR binding to Cav1.2 residues 1923–1942 is required for β-adrenergic regulation of Cav1.2. Despite the protein kinase A (PKA)-mediated phosphorylation of Cav1.2 S1928 within the newly identified β2AR binding site, its physiological function has escaped identification. They show that the phosphorylation of S1928 displaces the β2AR from Cav1.2 upon β-adrenergic stimulation rendering Cav1.2 refractory for several minutes from further β-adrenergic stimulation. These authors conclude that displacement of the β2AR from Cav1.2 is a uniquely specific desensitization mechanism of Cav1.2 regulation by localized β2AR/cAMP/PKA/S1928 signaling.
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