Fig. 2
From: Control of glutamate release by complexes of adenosine and cannabinoid receptors
Heteromeric and homomeric interfaces in the A2AR-CB1R heterotetramer. a–f BiFC experiments with synthetic peptides with the amino acid sequence of all TMs of A2AR and CB1R. HEK-293T cells were transiently transfected with a, b cDNAs of A2AR and CB1R separately fused to complementary halves of YFP (A2AR-cYFP and CB1-nYFP; 6 μg in both cases); c, e cDNAs of two different molecules of A2AR separately fused to complementary halves of YFP (A2AR-cYFP and A2AR-nYFP; 3 μg in both cases) without (c) or with (e) co-transfection with cDNA of non-fused CB1R (1 μg); d, f cDNAs of two different molecules of CB1R separately fused to complementary halves of YFP (CB1R-cYFP and CB1R-nYFP; 3 μg in both cases) without (d) or with (f) co-transfection with cDNA of non-fused A2AR (1 μg). Cells were treated for 4 h with medium (control) or 4 μM of indicated TM peptides (numbered 1–7). Values are means ± S.E.M. (n = 6 with triplicates in all the experiments) of the percentage of the fluorescence in the control group and analyzed statistically with repeated measures ANOVA, followed by Dunnett’s multiple comparison test (***: p < 0.001, compared with control)