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Fig. 5 | Molecular Neurodegeneration

Fig. 5

From: ULK1-mediated phosphorylation of ATG14 promotes autophagy and is impaired in Huntington’s disease models

Fig. 5

Proteotoxic stress causes a decrease in ATG14 phosphorylation and a redistribution of ULK1 into insoluble fraction. a ATG14 phosphorylation after proteasome inhibition. Phosphorylation of p62 is at S409. MEF cells were treated with MG132 for 16 h then separated into Triton X-100 soluble and insoluble fractions. b Quantification of ATG14 phosphorylation. ***p < 0.001 (n = 3). Data are represented as mean +/− SEM. c ULK1 accumulates in the Triton X-100 insoluble fraction in the brains of Q175 mice. d Quantification of ULK1 in the insoluble fraction. *p < 0.05 (n = 3). Data are represented as mean +/− SEM. e ATG14 phosphorylation after proteasome inhibition. P62 WT or KO MEF cells were treated with MG132 for 16 h then separated into Triton X-100 soluble and insoluble fractions. f Quantification of ATG14 phosphorylation in the soluble fraction. Two-way ANOVA was performed. Main effect of MG132 F(1, 8) = 92.60, p < 0.0001; Main effect of p62 KO F(1, 8) = 0.56, p = 0.4748; Interaction F(1, 8) = 7.82, p = 0.0233. (n = 3). Data are represented as mean +/− SEM. g Quantification of ULK1 in the insoluble fraction. Main effect of MG132 F(1, 8) = 252.94, p < 0.0001; Main effect of p62 KO F(1, 8) = 87.94, p < 0.0001; Interaction F(1, 8) = 81.33, p < 0.0001 (n = 3). Data are represented as mean +/− SEM

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