Abstract
Despite some caveats, G protein-coupled receptor oligomerization is a phenomenon that is becoming largely accepted. Within these oligomers, however, stoichiometry remains to be elucidated. Here, by using bimolecular fluorescence complementation, we visualized adenosine A 2A receptor homodimers in living cells, showing no apparent difference in the subcellular distribution when compared to the YFP-labelled adenosine A 2A receptor protomer. Interestingly, the combination of bimolecular fluorescence complementation and bioluminescence resonance energy transfer techniques allowed us to detect the occurrence of adenosine A 2A receptors oligomers containing more than two protomers. These results provide new insights into the molecular composition of G protein-coupled receptor oligomers. Structured summary MINT- 6700472: A2A (uniprotkb: P29274), A2A (uniprotkb: P29274) and A2A (uniprotkb: P29274) physically interact (MI: 0218) by bioluminescence resonance energy transfer (MI: 0012) MINT- 6699330: A2A (uniprotkb: P29274) and A2A (uniprotkb: P29274) physically interact (MI: 0218) by bimolecular fluorescence complementation (MI: 0809) MINT- 6699346: A2A (uniprotkb: P29274) and A2A (uniprotkb: P29274) physically interact (MI: 0218) by bioluminescence resonance energy transfer (MI: 0012)
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