Journal: bioRxiv

Article Title: Distinct TAF15 amyloid filament folds define multiple subtypes of FTLD-TAF15

doi: 10.64898/2026.01.12.698957

Figure Lengend Snippet: a-c, Cryo-EM reconstructions (black outlines) and atomic models of variants I (a) , II (b) and III (c) of TAF15 filament fold B, shown for a single TAF15 molecule perpendicular to the helical axis. The cryo-EM reconstructions are shown using a surface zone around the atomic models. The atomic models are colour-coded as a gradient from N– to C-terminal residues. Central slices of the cryo-EM reconstructions centred on the helical axis are shown as inserts. A disconnected TAF15 Y135-N145 peptide (cyan arrow), lipid-like densities (magenta arrow) and large round disconnected densities (yellow arrow) are highlighted.

Article Snippet: Immunohistochemistry was performed on 5 μm-thick paraffin-embedded, formalin-fixed tissue sections using antibodies against FUS (Proteintech 60160-1-Ig) at a dilution of 1:2,000; TAF15 (Bethyl IHC-00094) at a dilution of 1:300; and α-internexin (Invitrogen 32-3600) at a dilution of 1:1,000 using a Ventana BenchMark GX automated staining system (Roche) using the optiVIEW DAB detection kit (Roche).

Techniques: Cryo-EM Sample Prep

Journal: bioRxiv

Article Title: Distinct TAF15 amyloid filament folds define multiple subtypes of FTLD-TAF15

doi: 10.64898/2026.01.12.698957

Figure Lengend Snippet: a-c, Cryo-EM reconstructions (black outlines) and atomic models of TAF15 filament fold F (a) , fold G (b) and fold H (c) , shown for a single TAF15 molecule perpendicular to the helical axis. The cryo-EM reconstructions are shown using a surface zone around the atomic models. The atomic models are colour-coded as a gradient from N– to C-terminal residues. The Y38C substitution in TAF15 fold H is indicated with a black arrow. Central slices of the cryo-EM reconstructions centred on the helical axis are shown as inserts. A disconnected peptide (cyan arrow) and a lipid-like density (magenta arrow) associated with fold F are highlighted. d, Insert of TAF15 filament fold H centred on the Y38C substitution.

Article Snippet: Immunohistochemistry was performed on 5 μm-thick paraffin-embedded, formalin-fixed tissue sections using antibodies against FUS (Proteintech 60160-1-Ig) at a dilution of 1:2,000; TAF15 (Bethyl IHC-00094) at a dilution of 1:300; and α-internexin (Invitrogen 32-3600) at a dilution of 1:1,000 using a Ventana BenchMark GX automated staining system (Roche) using the optiVIEW DAB detection kit (Roche).

Techniques: Cryo-EM Sample Prep

Journal: bioRxiv

Article Title: Distinct TAF15 amyloid filament folds define multiple subtypes of FTLD-TAF15

doi: 10.64898/2026.01.12.698957

Figure Lengend Snippet: a-d, Cryo-EM reconstructions (black outlines) and atomic models of TAF15 filament fold C (a) , fold D (b) , fold D’ (c) and fold E (d) , shown for a single TAF15 molecule perpendicular to the helical axis. The cryo-EM reconstructions are shown using a surface zone around the atomic models. The atomic models are colour-coded as a gradient from N– to C-terminal residues. Central slices of the cryo-EM reconstructions centred on the helical axis are shown as inserts. A disconnected peptide (cyan arrow) and large round disconnected density (yellow arrow) associated with folds D and D’ are highlighted.

Article Snippet: Immunohistochemistry was performed on 5 μm-thick paraffin-embedded, formalin-fixed tissue sections using antibodies against FUS (Proteintech 60160-1-Ig) at a dilution of 1:2,000; TAF15 (Bethyl IHC-00094) at a dilution of 1:300; and α-internexin (Invitrogen 32-3600) at a dilution of 1:1,000 using a Ventana BenchMark GX automated staining system (Roche) using the optiVIEW DAB detection kit (Roche).

Techniques: Cryo-EM Sample Prep

Journal: bioRxiv

Article Title: Distinct TAF15 amyloid filament folds define multiple subtypes of FTLD-TAF15

doi: 10.64898/2026.01.12.698957

Figure Lengend Snippet: a, Main chain traces of TAF15 filament folds (A-H) and their variants (I-III) from aFTLD-U, NIFID (cases 1-11) and BIBD (cases 1-3). The Y38C substitution in TAF15 fold H from BIBD case 3 is highlighted. Residues are colour-coded as a gradient from N– to C-terminal. b, Amino acid sequence alignment of the secondary structure elements of the TAF15 filament folds (A-H) and their variants (I-III). Arrows indicate β-strands, which are colour-coded as a gradient from N– to C-terminal.

Article Snippet: Immunohistochemistry was performed on 5 μm-thick paraffin-embedded, formalin-fixed tissue sections using antibodies against FUS (Proteintech 60160-1-Ig) at a dilution of 1:2,000; TAF15 (Bethyl IHC-00094) at a dilution of 1:300; and α-internexin (Invitrogen 32-3600) at a dilution of 1:1,000 using a Ventana BenchMark GX automated staining system (Roche) using the optiVIEW DAB detection kit (Roche).

Techniques: Sequencing

Journal: bioRxiv

Article Title: Distinct TAF15 amyloid filament folds define multiple subtypes of FTLD-TAF15

doi: 10.64898/2026.01.12.698957

Figure Lengend Snippet: a, Immunohistochemistry for TAF15 (brown) in prefrontal cortex sections from aFTLD-U cases 1-3 with TAF15 filament fold A; NIFID cases 4, 6 and 7 with TAF15 fold B; NIFID cases 9-11 with TAF15 folds C-E, respectively; and BIBD cases 1-3 with TAF15 folds F-H, respectively. Sections were counterstained with haematoxylin (blue). The predominant TAF15-immunoreactive neuronal cytoplasmic inclusions (NCIs) in aFTLD-U cases are compact round (cyan arrows). NIFID cases with fold B are characterised by a predominance of compact round NCIs and the presence of neuropil dots (magenta arrow). NIFID cases with folds C-E and BIBD cases with folds F-H show a predominance of annular and tangle-like NCIs (yellow arrows) and the presence of dystrophic neurites (DN, green arrows). Case numbers are indicated at the top left of the images. Scale bar, 25 µm. b, Graph of semi-quantitative scoring of TAF15-immunoreactive cytoplasmic inclusion types among NIFID cases with fold B (n=8), NIFID cases with folds C-E (n=3) and BIBD cases with folds F-H (n=3) from Supplementary Table 3. Individual datapoints and means ± SD are shown. *p<0.05, **p<0.01, ***p<0.001, (Kruskal-Wallis test with Dunn’s post-hoc test). c, Heatmap of correlation (Pearson’s r ) among semi-quantitative scoring of TAF15-immunoreactive cytoplasmic inclusion types in the aFTLD-U (n=3), NIFID (n=11) and BIBD (n=3) cases from Supplementary Table 3. Crosses indicate that the values for both variables are identical, precluding correlation analysis. The TAF15 filament folds (A-H) of the cases are indicated.

Article Snippet: Immunohistochemistry was performed on 5 μm-thick paraffin-embedded, formalin-fixed tissue sections using antibodies against FUS (Proteintech 60160-1-Ig) at a dilution of 1:2,000; TAF15 (Bethyl IHC-00094) at a dilution of 1:300; and α-internexin (Invitrogen 32-3600) at a dilution of 1:1,000 using a Ventana BenchMark GX automated staining system (Roche) using the optiVIEW DAB detection kit (Roche).

Techniques: Immunohistochemistry

Journal: International Journal of Biological Sciences

Article Title: The SOX10-ACAT2-Cholesterol Synthesis Axis Is Required for Melanoma Proliferation

doi: 10.7150/ijbs.114084

Figure Lengend Snippet: The SOX10-TAF15 interaction drives ACAT2 transcriptional activation. (a) ChIP-qPCR analysis of SOX10 binding to potential sites in the ACAT2 promoter in SK-MEL-28 cells using anti-SOX10 or IgG antibody. (b) Schematic diagram of promoter mutation sites. (c) Luciferase activity of wild-type or mutant ACAT2 promoter reporters in SK-MEL-28 cells expressing empty vector (EV) or SOX10. (d-g) Co-immunoprecipitation assays in HEK293T cells co-transfected with Flag-SOX10 and HA-TAF15 (d, e) or in SK-MEL-28 and CM2005.1 cells (f, g), using equal protein amounts for immunoprecipitation with the indicated antibodies, followed by immunoblotting with anti-HA (d) , anti-Flag (e) , anti-TAF15 (f) , or anti-SOX10 (g) antibody. (h) QRT-PCR analysis of ACAT2 expression in SK-MEL-28 cells with TAF15 overexpression or knockdown. (i) Western blot analysis of ACAT2 and TAF15 expression in SK-MEL-28 cells with TAF15 overexpression or knockdown. (j) Luciferase activity of the ACAT2 promoter reporter in SK-MEL-28 cells expressing EV or TAF15. (k) Luciferase activity of the ACAT2 promoter reporter in SOX10-overexpressing SK-MEL-28 cells further infected with shTAF15 or non-targeting control (NTC) virus. Data are presented as mean ± SD from three independent experiments. *P < 0.05 compared to the indicated control groups in each panel by one-way ANOVA with Bonferroni post-hoc test. Actin served as a loading control in (d-g, i). See also .

Article Snippet: The following primary antibodies were used: anti-HMGCR, anti-SOAT1 (Abcam), anti-Flag M2 (Sigma-Aldrich), anti-ACAT2, anti-HMGCS1, anti-IDI1, anti-FDPS, anti-ACAT1, anti-SOX10, anti-TAF15, and anti-β-actin (Proteintech).

Techniques: Activation Assay, ChIP-qPCR, Binding Assay, Mutagenesis, Luciferase, Activity Assay, Expressing, Plasmid Preparation, Immunoprecipitation, Transfection, Western Blot, Quantitative RT-PCR, Over Expression, Knockdown, Infection, Control, Virus