Fig. 4
HDAC5 directly interacts with SOX9. a Co-immunoprecipitation in MCF-7 cells with anti-Flag HDAC5 followed by immunoblotting with an antibody against MYC–SOX9. b Co-immunoprecipitation assay in MCF-7 cells with anti-MYC SOX9 followed by immunoblotting with an antibody against Flag–HDAC5. c Immunoprecipitation in TAMR MCF-7 cells with anti-SOX9 followed by immunoblotting with an antibody against HDAC5. d Immunoprecipitation in TAMR T47D cells with anti-SOX9 followed by immunoblotting with an antibody against HDAC5. e Immunoprecipitation in parental and TAMR MCF-7 cells with anti-HDAC5 followed by immunoblotting with an antibody against SOX9. f Immunoprecipitation in parental and TAMR T47D cells with anti-HDAC5 followed by immunoblotting with an antibody against SOX9. g Co-immunoprecipitation assay in MCF-7 cells transfected with plasmid containing SOX9 HMGB domain or TA domain with anti-Flag-M2 beads followed by immunoblotting with an antibody against HA. Top: schematic diagram of full-length SOX9 and truncated mutants. h Co-immunoprecipitation assay in MCF-7 cells transfected with plasmid containing HDAC5 MEF2 binding domain or NLS domain, HDAC domain with anti-Flag-M2 beads followed by immunoblotting with an antibody against SOX9. Top: schematic diagram of full-length HDAC5 and truncated mutants. Scale bar, 20 μm. Data are representative of at least three independent experiments
