A Naturally Occurring Splice Variant of GGA1 Inhibits the Anterograde Post-Golgi Traffic of α_2B-Adrenergic Receptor.

ABSTRACT: The regulatory mechanisms of cell surface targeting of nascent G protein-coupled receptors (GPCRs) en route from the endoplasmic reticulum through the Golgi remain poorly understood. We have recently demonstrated that three Golgi-localized, γ-adaptin ear domain homology, ADP ribosylation factor-binding proteins (GGAs) mediate the post-Golgi export of α_2B-adrenergic receptor (α_2B-AR), a prototypic GPCR, and directly interact with the receptor. In particular, GGA1 interaction with α_2B-AR is mediated via its hinge domain. Here we determined the role of a naturally occurring truncated form of GGA1 (GGA1t) which lacks the N-terminal portion of the hinge domain in α_2B-AR trafficking and elucidated the underlying mechanisms. We demonstrated that both GG

SUBMITTER: Zhang M 

PROVIDER: S-EPMC6637153 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature