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• W2611083600 endingPage "2018" @default.
• W2611083600 startingPage "2004" @default.
• W2611083600 abstract "N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs). However, it remains unknown how N-glycosylation affects GPCR signaling. β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2). Here, we show that deletion of the N-glycan did not affect receptor expression and ligand binding. Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization. Both N6Q and N15Q showed decreased receptor dimerization, while N187Q did not influence receptor dimerization. As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization. To verify this hypothesis, we further paid attention to the residues at the dimerization interface. Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function. This work provides new insights into the relationship among glycosylation, dimerization, and function of GPCRs.Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96)." @default.
• W2611083600 created "2017-05-12" @default.
• W2611083600 creator A5033199641 @default.
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• W2611083600 date "2017-05-25" @default.
• W2611083600 modified "2023-10-14" @default.
• W2611083600 title "N-glycosylation of the β₂adrenergic receptor regulates receptor function by modulating dimerization" @default.
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• W2611083600 doi "https://doi.org/10.1111/febs.14098" @default.
• W2611083600 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28467637" @default.
• W2611083600 hasPublicationYear "2017" @default.
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