Fig. 2: K136 mutations reduce the solubility of TDP-43 and trigger its ubiquitination and pathological phosphorylation. | Nature Communications

Fig. 2: K136 mutations reduce the solubility of TDP-43 and trigger its ubiquitination and pathological phosphorylation.

From: Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43

Fig. 2

a HEK293E shTDP-43 cells were transfected with 6xHis-tagged TDP-43 (wt, K136R and K136Q) or Flag-tagged FFLL TDP-43. RIPA soluble and insoluble fractions were separated and analyzed by Western blotting. N = 3 biologically independent samples. Source data are provided as a Source Data file. b ShTDP-43-HEK293E cells were transfected with 6xHis-tagged TDP-43 (wt, K136R and K136Q). Proteasome activity was inhibited by treatment with 20 µM MG-132 for 6 h, which caused wtTDP-43 ubiquitination (lane 3). 6xHis-tagged TDP-43 was purified with NiNTA beads and analyzed on Western blots. N = 3 biologically independent samples. Source data are provided as a Source Data file. c Transfected shTDP-43-HEK293E cells were double immunostained for TDP-43 and phosphorylated TDP-43 (S409/410). Scale bar represents 10 μm. N = 3 biological replicates.

Back to article page