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. Author manuscript; available in PMC: 2012 Feb 25.
Published in final edited form as: J Mol Biol. 2011 Jan 6;406(3):467–478. doi: 10.1016/j.jmb.2010.12.034

Figure 3. Exchange of the structurally different C-domain receptor-binding element between arrestin-2 and -3 changes their binding to ß2AR in intact cells.

Figure 3

Figure 3

A. BRET signal as a function of WT Venus-arrestin-2 (filled circles, solid line) and the Venus-arrestin-2-6M mutant (I233V, N245S, M255Q, E256V, A258Q and T261Q; open circles, dashed line) co-expression with ß2AR-RLuc in COS-7 cells. B. BRET signal as a function of WT Venus-arrestin-3 (filled triangles, solid line) and the Venus-arrestin-3-6M mutant (V234I, S246N, Q256M, V257E, Q259A and Q262A; open circles, dashed line) co-expression with ß2AR-RLuc in COS-7 cells. Shown is the difference between BRET signal in the presence and absence of 25 μM ß2AR agonist isoproterenol, which reflects agonist-induced increase in Venus-arrestin interaction with fixed amount of ß2AR-RLuc. Means ± SE of one representative experiment (out of three) performed in quadruplicate are shown in A and B. C. The average BRETMAX as estimated from the fits of a one-site binding hyperbola to the data of the binding of the indicated arrestins to the ß2AR. Means ± S.E. of three independent experiments are shown. The differences between the BRETMAX values were assessed by one-way ANOVA, followed by Bonferroni post hoc test. Significance of the differences is indicated as follows: *p<0.05, **p<0.01, ***p<0.001.