Fig. 4

FAM171B interacts with vimentin and HNRNPU in bladder cancer cells. A Mass spectrometry analysis of interacting proteins enriched by immunoprecipitation. Immunoprecipitation is performed by Anti-DYKDDDDK beads on T24 cells transfected with FLAG-FAM171B or FLAG-control. B Analysis of positive and background proteins based on Mass Spectrometry scores. C The top 16 proteins with the highest scores based on MS results. D Protein interaction network map of proteins bound to FAM171B based on MS results. The protein interactions data is from STRING database. E The predicted protein structure image of FAM171B based on the Alpha Fold. F Immunofluorescence analysis images revealed the localization of FAM171B in T24 cells. G Colocalization of FAM171B and vimentin was visualized by confocal microscope in T24 cells. Cytoplasmic staining of FAM171B and vimentin was mostly merged together. H Colocalization of FAM171B and HNRNPU was visualized by confocal microscope in T24 cells. Nuclear staining of FAM171B and HNRNPU was mostly merged together. I ImageJ was used for colocation analysis of FAM171B and vimentin. Pearson correlation analysis showed that r > 0.5. Manders’ colocation coefficient showed that M1 > 0.5 and M2 > 0.5. J Computational docking model between FAM171B and vimentin. K ImageJ was used for colocation analysis of FAM171B and HNRNPU. Pearson correlation analysis showed that r > 0.5. Manders’ colocation coefficient showed that M1 > 0.5 and M2 > 0.5. L Computational docking model between FAM171B and HNRNPU