Effect of G3BP1 and IMP1 deletions on protein exchange between SGs. (A and B) FDAP curves for PAGFP-G3BP1C (A) and PAGFP-IMP1C (B; mean ± SEM, n = 22 and n = 13, respectively). Schematic representations of the deletion constructs are shown on top. Protein interaction (gray) and RNA-binding domains (black) are indicated. Residence time of PAGFP-tagged G3BP1C (A) and PAGFP-IMP1C (B) in granules as determined by the model FDAP function (mean ± SEM, n = 22 from four and n = 13 from six independent experiments, respectively) are shown on the right. Values for full-length PAGFP-G3BP1 and PAGFP-IMP1 from Fig. 1 are indicated for comparison by dotted lines (green and red, respectively). The deletion constructs were not showing statistically significant differences to their respective full-length counterparts, but were statistically significantly different from the control construct (3×PAGFP vs. PAGFP-G3BP1C, P < 0.05; 3×PAGFP vs. PAGFP-IMP1C, P < 0.001). Statistics involved one-way ANOVA followed by post-hoc Tukey's test. Bars, 20 µm. For all experiments, stress had been induced by a 20-min treatment with 0.5 mM sodium arsenite before imaging.
