Figure 3.
Pairwise binding reveals the relative occupancies of different Kaps. (A) exoCRM1 titration in the presence of 10 μM exoKapβ1. (B) Normalized fluorescence signals of exoCRM1 and exoKapβ1 plotted as a function of exoCRM1 concentration. The maximal observed change in the relative occupancy of exoCRM1 is obtained by subtracting its titration value (blue) from its standalone value (gray) at the highest concentration (i.e., 10 μM exoCRM1; blue arrow). The relative occupancy of exoKapβ1 obtained in the presence of 10 μM exoCRM1 is also shown (green arrow). A single-component Langmuir isotherm fit provides the KD,NPC of exoCRM1 in the presence of 10 μM exoKapβ1. (C) exoImp5 titration in the presence of 10 μM exoKapβ1. (D) Normalized fluorescence signals of exoImp5 and exoKapβ1 plotted as a function of exoImp5 concentration. The maximal observed change in the relative occupancy of exoImp5 is obtained by subtracting its titration value (magenta) from its standalone value (gray) at 10 μM exoImp5 (magenta arrow). The relative occupancy of exoKapβ1 obtained in the presence of 10 μM exoImp5 is also shown (green arrow). (E) Titration of exoImp5 in the presence of 10 μM exoCRM1. (F) Normalized fluorescence signals of exoImp5 and exoCRM1 plotted as a function of exoImp5 concentration. The maximal observed change in the relative occupancy of exoImp5 is obtained by subtracting its titration value (magenta) from its standalone value (gray) at 10 μM exoImp5 (magenta arrow). The relative occupancy of exoCRM1 obtained in the presence of 10 μM exoImp5 is also shown (blue arrow). Cells in the first row are visualized within the dynamic range shown. The brightness has been adjusted in each second row to better visualize the nuclear rim. Percentages above the panels indicate the laser power used to image the cells. Data points, error bars, and KD,NPC values were obtained by propagating means and errors across all replicates (n ≥ 3). Scale bars, 20 µm.

Pairwise binding reveals the relative occupancies of different Kaps. (A) exoCRM1 titration in the presence of 10 μM exoKapβ1. (B) Normalized fluorescence signals of exoCRM1 and exoKapβ1 plotted as a function of exoCRM1 concentration. The maximal observed change in the relative occupancy of exoCRM1 is obtained by subtracting its titration value (blue) from its standalone value (gray) at the highest concentration (i.e., 10 μM exoCRM1; blue arrow). The relative occupancy of exoKapβ1 obtained in the presence of 10 μM exoCRM1 is also shown (green arrow). A single-component Langmuir isotherm fit provides the KD,NPC of exoCRM1 in the presence of 10 μM exoKapβ1. (C) exoImp5 titration in the presence of 10 μM exoKapβ1. (D) Normalized fluorescence signals of exoImp5 and exoKapβ1 plotted as a function of exoImp5 concentration. The maximal observed change in the relative occupancy of exoImp5 is obtained by subtracting its titration value (magenta) from its standalone value (gray) at 10 μM exoImp5 (magenta arrow). The relative occupancy of exoKapβ1 obtained in the presence of 10 μM exoImp5 is also shown (green arrow). (E) Titration of exoImp5 in the presence of 10 μM exoCRM1. (F) Normalized fluorescence signals of exoImp5 and exoCRM1 plotted as a function of exoImp5 concentration. The maximal observed change in the relative occupancy of exoImp5 is obtained by subtracting its titration value (magenta) from its standalone value (gray) at 10 μM exoImp5 (magenta arrow). The relative occupancy of exoCRM1 obtained in the presence of 10 μM exoImp5 is also shown (blue arrow). Cells in the first row are visualized within the dynamic range shown. The brightness has been adjusted in each second row to better visualize the nuclear rim. Percentages above the panels indicate the laser power used to image the cells. Data points, error bars, and KD,NPC values were obtained by propagating means and errors across all replicates (n ≥ 3). Scale bars, 20 µm.

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