Fig. 5: Putative phosphate ion pore.
From: Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate
Plots of the pore radius as a function of the pore axis of XPR1IN (a) and XPR1OUT (b). The pore-lining surfaces were calculated using the program HOLE257 and depicted on ribbon models of the XPR1IN (a) and XPR1OUT (b). c The phosphate ion transport pore of XPR1OUT. The critical regions of the pore are labeled with dotted boxes. The extracellular views (d, e) and intracellular view (f) of the cross sections through the ion-transporting pore at indicated positions in (c). The ribbon is colored as in (c). The conserved pore-lining residues are shown in sticks and colored in magenta. g, h 32Pi efflux of EV, WT-XPR1 and XPR1 mutants in the phosphate ion transport pores. The numbers of biologically independent experiments are identical with (i). i 32P efflux percentages of EV and XPR1 mutants in (g, h) at 2 h normalized against WT-XPR1. From left to right: n = 4, 24, 3, 3, 3, 3, 3, 3, 3, 3, 4, 3, and 3 biologically independent experiments. P values are 4 × 10−4, 1, 0.1552, 0.5686, <1 × 10−4, 1.4 × 10−3, <1 × 10−4, <1 × 10−4, 2.8 × 10−3, <1 × 10−4, <1 × 10−4, <1 × 10−4, and <1 × 10−4. Data are shown as mean ± s.d. in (g–i). P values were obtained by a two-tailed unpaired t-test with Welch’s correction in (i).
