Fig. 2: dFUS-E9C interacts with RGG2 and RRM domains of FUS.
From: DNA nanoflower Oligo-PROTAC for targeted degradation of FUS to treat neurodegenerative diseases
a A summary of tested FUS truncation mutants and their affinity to dFUS-E9C. b Streptavidin pulldown assays to determine the binding capability between Biotin-dFUS-E9C and FUS truncations. c, d Predicted interactions of RRG2 (c) or RRM (d) domain with dFUS-E9C by molecular simulation. Red bases are predicted to be critical for the interaction between the Oligo and FUS. e The critical bases of FUS-RNA#E9 responsible for FUS binding were mutated and marked in red. f MST assays to determine the binding affinity of GFP-FUS to dFUS-E9C and its mutants. g Streptavidin pulldown assays to assess the interaction between FUS and Biotin-dFUS-E9 and its mutants. h, i Immunoblots (h) and quantitative analysis (i) of PC12, SH-SY5Y, and Neuro-2a cells transfected with increasing concentrations of dFUS-E9C for 24 h. The averages of n = 3 (f, i) biologically independent samples are shown. Data are shown as the mean ± SEM. The data presented in (b, g, h) are representative of three independent experiments. Source data are provided as a Source Data file.
