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• W2041211150 abstract "G protein-coupled receptors (GPCRs) respond to a diverse array of ligands, mediating cellular responses to hormones and neurotransmitters, as well as the senses of smell and taste. The structures of the GPCR rhodopsin and several G proteins have been determined by x-ray crystallography, yet the organization of the signaling complex between GPCRs and G proteins is poorly understood. The observations that some GPCRs are obligate heterodimers, and that many GPCRs form both homo- and heterodimers, has led to speculation that GPCR dimers may be required for efficient activation of G proteins. However, technical limitations have precluded a definitive analysis of G protein coupling to monomeric GPCRs in a biochemically defined and membrane-bound system. Here we demonstrate that a prototypical GPCR, the β 2 -adrenergic receptor (β 2 AR), can be incorporated into a reconstituted high-density lipoprotein (rHDL) phospholipid bilayer particle together with the stimulatory heterotrimeric G protein, Gs. Single-molecule fluorescence imaging and FRET analysis demonstrate that a single β 2 AR is incorporated per rHDL particle. The monomeric β 2 AR efficiently activates Gs and displays GTP-sensitive allosteric ligand-binding properties. These data suggest that a monomeric receptor in a lipid bilayer is the minimal functional unit necessary for signaling, and that the cooperativity of agonist binding is due to G protein association with a receptor monomer and not receptor oligomerization." @default.
• W2041211150 created "2016-06-24" @default.
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• W2041211150 date "2007-05-01" @default.
• W2041211150 modified "2023-10-16" @default.
• W2041211150 title "A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein" @default.
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• W2041211150 doi "https://doi.org/10.1073/pnas.0611448104" @default.
• W2041211150 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1863461" @default.
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• W2041211150 hasPublicationYear "2007" @default.
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