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. 2020 Nov 1;31(23):2522–2536. doi: 10.1091/mbc.E20-05-0290

FIGURE 8:

FIGURE 8:

Phosphomimetic substitution reduces FUS solid-phase aggregation in vitro. (A) Differential interference microscopy of full-length and phosphomimetic variants of FUS (4Ev3, 4Ev4, or 12E). Maltose binding protein (MBP)–tagged FUS proteins were agitated for 1 day at 25°C after the addition of TEV protease. (B) Turbidity assay of full-length FUS in the presence of varying salt concentrations. Turbidity was assessed 45 min following TEV addition (n = 10). Two-way ANOVA was used for statistical analysis (*indicates significance relative to 150 mM NaCl).