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. 2014 Nov 5;467(9):1919–1929. doi: 10.1007/s00424-014-1636-6

Fig. 6.

Fig. 6

α2δ-1 is necessary for the USP2-45-induced decrease of Cav1.2 currents. a, b Representative whole-cell current traces and corresponding bar graphs showing that USP2-45 failed to regulate Cav1.2 channels in the absence of α2δ-1 subunits (a), whereas USP2-45 still decreases Cav1.2 currents in the absence of β2 (b). tsA-201 cells were transfected with Cav1.2/β2 alone (white circle, (control)) or together with USP2-45 (black circle) in a and Cav1.2/α2δ-1 alone (white square (control)) or together with USP2-45 (black square) in b. As expected because of their known involvement in Cav trafficking, the absence of either subunit decreased Cav current densities (compared to Fig. 1). The lack of β subunit in particular dramatically decreased Cav currents, despite the charge carrier being increased to 20 mM BaCl2 in order to reliably quantify the decrease caused by USP2-45 on Cav1.2/α2δ-1 channels. The data show the amplitude of the current densities recorded at 20 mV which generates the maximal current in the absence of β. As for prior experiments, 5 mM BaCl2 was used to record Cav1.2/β2 currents. Currents densities are compared at 10 mV which generates the maximal current in the absence of α2δ-1. The number of cells is indicated in parentheses. NS non-significant. *p < 0.05 when compared with respective control