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• W2078482767 endingPage "2927" @default.
• W2078482767 startingPage "2920" @default.
• W2078482767 abstract "G protein-coupled receptors (GPCRs) interact directly with heterotrimeric G proteins to transduce physiological signals. Early studies of this interaction concluded that GPCRs (R) and G proteins (G) collide with each other randomly after receptor activation and that R-G complexes are transient. More recent studies have suggested that inactive R and G are preassembled (precoupled) as stable R-G complexes. Here we examine the stability of complexes formed between cyan fluorescent protein-labeled alpha(2A)-adrenoreceptors (C-alpha2ARs) and G proteins in cells using fluorescence recovery after photobleaching (FRAP). Labeled G proteins diffused in the plasma membrane with equal mobility in the absence and presence of immobile C-alpha2ARs. Immobile C-alpha2ARs activated labeled G proteins, demonstrating functional coupling without stable physical association. In contrast, a stable R-G interaction was detected when G proteins were deprived of nucleotides and C-alpha2ARs were active, as predicted by the ternary complex model. Overexpression of regulator of G protein signaling 4 (RGS4) accelerated the onset of effector activation but did not detectably alter the interaction between C-alpha2ARs and G proteins. We conclude that at most a small fraction of C-alpha2ARs and G proteins exist as R-G complexes at any moment." @default.
• W2078482767 created "2016-06-24" @default.
• W2078482767 creator A5004277635 @default.
• W2078482767 creator A5025823909 @default.
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• W2078482767 date "2008-04-23" @default.
• W2078482767 modified "2023-10-16" @default.
• W2078482767 title "Abundance and stability of complexes containing inactive G protein‐coupled receptors and G proteins" @default.
• W2078482767 cites W1565088438 @default.
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• W2078482767 doi "https://doi.org/10.1096/fj.08-105775" @default.
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• W2078482767 hasPublicationYear "2008" @default.
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