Title : S-Palmitoylation of a Novel Site in the β2-Adrenergic Receptor Associated with a Novel Intracellular Itinerary.

Pub. Date : 2016 Sep 16

PMID : 27481942






5 Functional Relationships(s)
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1 We report here that a population of human beta2-adrenergic receptors (beta2AR), a canonical G protein-coupled receptor, traffics along a previously undescribed intracellular itinerary via the Golgi complex that is associated with the sequential S-palmitoylation and depalmitoylation of a previously undescribed site of modification, Cys-265 within the third intracellular loop. Cysteine adrenoceptor beta 2 Homo sapiens
2 We report here that a population of human beta2-adrenergic receptors (beta2AR), a canonical G protein-coupled receptor, traffics along a previously undescribed intracellular itinerary via the Golgi complex that is associated with the sequential S-palmitoylation and depalmitoylation of a previously undescribed site of modification, Cys-265 within the third intracellular loop. Cysteine adrenoceptor beta 2 Homo sapiens
3 In addition, beta2AR S-palmitoylated at Cys-265 are selectively preserved under a sustained adrenergic stimulation, which results in the down-regulation and degradation of betaAR. Cysteine adrenoceptor beta 2 Homo sapiens
4 Cys-265 is not conserved in beta1AR, and S-palmitoylation of Cys-265 may thus be associated with functional differences between beta2AR and beta1AR, including relative resistance of beta2AR to down-regulation in multiple pathophysiologies. Cysteine adrenoceptor beta 2 Homo sapiens
5 Cys-265 is not conserved in beta1AR, and S-palmitoylation of Cys-265 may thus be associated with functional differences between beta2AR and beta1AR, including relative resistance of beta2AR to down-regulation in multiple pathophysiologies. Cysteine adrenoceptor beta 2 Homo sapiens