Journal
EMBO REPORTS
Volume 9, Issue 4, Pages 363-369Publisher
WILEY
DOI: 10.1038/embor.2008.27
Keywords
asymmetry; dimerization; GPCR; receptor; serotonin
Categories
Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R01 GM068671, GM68671] Funding Source: Medline
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G-protein-coupled receptors (GPCRs) respond to external stimuli by activating heterotrimeric G proteins inside the cell. There is increasing evidence that many GPCRs exist as dimers or higher oligomers, but the biochemical nature of such dimers and what roles they have, if any, in signal transduction remains unclear. We conducted a comprehensive study of dimerization of the 5HT2c serotonin receptor using disulphide-trapping experiments. We found a dimer interface between transmembrane (TM) helices IV and V that is markedly sensitive to the state of receptor activation. This dimer seems to be quasisymmetrical in interfacial geometry and asymmetrical in its association with its cognate G alpha protein. We also found a second interface at TM I helices, which is insensitive to the state of activation.
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