期刊
FASEB JOURNAL
卷 34, 期 12, 页码 16348-16363出版社
WILEY
DOI: 10.1096/fj.202001355RR
关键词
cell surface trafficking; coiled-coil domain; endoplasmic reticulum retention; GPCR
资金
- Ministry of Science and Technology of the People's Republic of China (MOST) [2018YFA0507003]
- National Natural Science Foundation of China (NSFC) [81720108031, 81872945, 31721002, 31420102909]
- Program for Introducing Talents of Discipline to the Universities of the Ministry of Education [B08029]
- Institut National de la Sante et de la Recherche Medicale (Inserm)
- Centre National de la Recherche Scientifique (CNRS)
- Program Hubert Curien (PHC) Cai Yuanpei
Cell surface trafficking of many G protein-coupled receptors is tightly regulated. Among them, the mandatory heterodimer GABA(B)receptor for the main inhibitory neurotransmitter, gamma-aminobutyric acid (GABA), is a model. In mammals, its cell surface trafficking is highly controlled by an endoplasmic reticulum retention signal in the C-terminal intracellular region of the GB1 subunit that is masked through a coiled-coil interaction with the GB2 subunit. Here, we investigate the molecular basis for the export of its homolog inDrosophila melanogasterthat regulates the circadian rhythm and sleep. In contrast to mammals, the endoplasmic retention signal is carried by GB2, while GB1 reaches the cell surface alone. NMR analysis showed that the coiled-coil domain that controls GABA(B)heterodimer formation is structurally conserved between flies and mammals, despite specific features. These findings show the adaptation of a similar quality control system during evolution for maintaining the subunit composition of a functional heterodimeric receptor.
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