Relationship between homo-oligomerization of a mammalian olfactory receptor and its activation state demonstrated by bioluminescence resonance energy transfer (BRET) - Archive ouverte HAL
Article Dans Une Revue Journal of Biological Chemistry Année : 2011

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.
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hal-02651231 , version 1 (29-05-2020)

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Serigne Fallou Wade, Agathe Espagne, Marie-Annick Persuy, Jasmina Vidic, Regine Monnerie, et al.. Relationship between homo-oligomerization of a mammalian olfactory receptor and its activation state demonstrated by bioluminescence resonance energy transfer (BRET). Journal of Biological Chemistry, 2011, 286 (17), pp.15252-15259. ⟨10.1074/jbc.M110.184580⟩. ⟨hal-02651231⟩
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