N-glycosylation of α_1D-adrenergic receptor N-terminal domain is required for correct trafficking, function, and biogenesis.

ABSTRACT: G protein-coupled receptor (GPCR) biogenesis, trafficking, and function are regulated by post-translational modifications, including N-glycosylation of asparagine residues. α_1D-adrenergic receptors (α_1D-ARs) - key regulators of central and autonomic nervous system function - contain two putative N-glycosylation sites within the large N-terminal domain at N65 and N82. However, determining the glycosylation state of this receptor has proven challenging. Towards understanding the role of these putative glycosylation sites, site-directed mutagenesis and lectin affinity purification identified N65 and N82 as bona fide acceptors for N-glycans. Surprisingly, we also report that simultaneously mutating N65 and N82 causes early termination of α_1D-AR between transmem

SUBMITTER: Janezic EM 

PROVIDER: S-EPMC7190626 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature