Site-specific O-Glycosylation by Polypeptide N-Acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) Co-regulates β₁-Adrenergic Receptor N-terminal Cleavage.

ABSTRACT: The β₁-adrenergic receptor (β₁AR) is a G protein-coupled receptor (GPCR) and the predominant adrenergic receptor subtype in the heart, where it mediates cardiac contractility and the force of contraction. Although it is the most important target for β-adrenergic antagonists, such as β-blockers, relatively little is yet known about its regulation. We have shown previously that β₁AR undergoes constitutive and regulated N-terminal cleavage participating in receptor down-regulation and, moreover, that the receptor is modified by O-glycosylation. Here we demonstrate that the polypeptide GalNAc-transferase 2 (GalNAc-T2) specifically O-glycosylates β₁AR at five residues in the extracellular N terminus, including the Ser-49 residue at the l

SUBMITTER: Goth CK 

PROVIDER: S-EPMC5377785 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature