Fig. 3
From: Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
TDP-43 acetylation-mimic aggregates recruit the degradative machinery and promote mitochondrial dysfunction. a Cells expressing aggregate-prone TDP-43-ΔNLS-K145Q were analyzed by double-labeling using ubiquitin, 20S proteasome, or p62 antibodies, and counterstained with DAPI (blue). White arrows highlight co-localization of ubiquitin, 20S proteasome, or p62 with TDP-43 aggregates. b Mouse TA muscles electroporated with TDP-43-ΔNLS-K145Q for 14 days were similarly analyzed using ubiquitin, 20S proteasome, and p62 antibodies. White arrows highlight prominent co-localization of TDP-43 aggregates with ubiquitin, 20S proteasome, or p62 in mouse muscles. c, d Mouse tissues were analyzed by immunoblotting (c) or microscopy (d) using ubiquitin or p62 antibodies, as well as the mitochondrial panel of antibody markers (COXIV, TOM20 and Cytochrome c). Scale bar = 50 μm
