Relationship between homo-oligomerization of a mammalian olfactory receptor and its activation state demonstrated by bioluminescence resonance energy transfer (BRET)
Résumé
G-protein-coupled receptor homo-oligomerization has been increasingly reported. However, little is known regarding the relationship between activation of the receptor and its associa- tion/conformationalstates.Themammalianolfactoryreceptors (ORs) belong to the G protein-coupled receptor superfamily. In this study, the homo-oligomerization status of the human OR1740 receptor and its involvement in receptor activation upon odorant ligand binding were addressed by co-immuno- precipitationandbioluminescenceresonanceenergytransfer approaches using crude membranes or membranes from dif- ferent cellular compartments. For the first time, our data clearly show that mammalian ORs constitutively self-associ- ate into homodimers at the plasma membrane level. This study also demonstrates that ligand binding mediates a con- formational change and promotes an inactive state of the OR dimers at high ligand concentrations. These findings support andvalidateourpreviouslyproposedmodelofORactivation/ inactivation based on the tripartite odorant-binding protein- odorant-OR partnership.
Domaines
Neurosciences [q-bio.NC]
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2013_Fallou Wade_Journal of Biological Chemistry_1.pdf (1.36 Mo)
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