Fig. 1: Interaction between TDP43 and PS1.

A PPI network interaction between PS1, APP, and TDP43. The representative image of the protein-protein interaction (PPI) network of PS1, APP, and TDP43, indicating potential interactions among these proteins. B Co-immunoprecipitation (Co-IP) of TDP43 and PS1. HeLa cells were co-transfected with TDP43 and PS1 plasmids. After sample collection, a Co-IP assay was performed using a PS1 antibody, followed by western blotting with a c-Myc antibody to detect the interaction between TDP43 and PS1. C Bioinformatics prediction of the binding site between TDP43 and PS1. The z-DOCK online platform predicted the optimal binding position between TDP43 and PS1. The surface interactions of the two proteins were subsequently analyzed using Discovery Studio. D Immunofluorescence co-localization of TDP43 and PS1. HeLa cells were transfected with LacZ as a blank control (Group 1) and co-transfected with TDP43 and PS1 (Group 2), as well as TDP43 and PS1 with the addition of γ-secretase inhibitor L685,458 1 h before transfection (Group 3). After 24 h, immunofluorescence analysis was performed to detect the interaction between TDP43 and PS1. DAPI was used to stain the cell nuclei, TDP43 was labeled with FITC to emit green fluorescence, and PS1 was labeled with PE to emit red fluorescence. The merge image shows the integration of all three channels. E Impact of the interaction of TDP43 and PS1 on the nuclear localization of TDP43. TDP43 and PS1 were overexpressed in NSC34 cells, after which the nucleus and cytosol were isolated. Finally, the expression of TDP43 in the nucleus and cytosol was detected by WB. F Grayscale values of endogenous TDP43. The grayscale values in the graphs were calculated using Image J software analysis, and data are presented as mean ± SD. Two-way ANOVA with post hoc Bonferroni correction, compared with nucleus. (n = 3 independent experiments; *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001, ns not significant).