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. 2020 Jul 9;10(19):8606–8618. doi: 10.7150/thno.46861

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FBP1 Ser144 phosphorylation regulates binding to p65. Immunoprecipitation and immunoblotting analyses were performed with the indicated antibodies. (A, B) 293T cells were transfected with indicated plasmids, followed by IP with anti-HA (a) or Flag (b) and IB with indicated antibodies. (C, D) MCF-7 cells were collected, followed by IP with anti-p65 (c) or FBP1 (d) and IB with indicated antibodies. (E) Purified GST-tagged p65 or GST was mixed with His-FBP1 for GST pull-down assay. (F) Confocal immunofluorescence microscopy was performed to analyze localization of FBP1 and p65 in MCF-7 cells. (G) The P65 truncation mutants used in this study. 293T cells were overexpressed the indicated HA-tagged FBP1 and GFP-tagged p65 fragments proteins. Immunoprecipitation with an anti-HA antibody was performed. (H, I) 293T cells were overexpressed the indicated HA-tagged p65 and GFP-tagged FBP1 fragments proteins. Immunoprecipitation with an anti-HA antibody was performed. (J) 293T cells were overexpressed the indicated HA-tagged FBP1 (WT, S144A or S144D) and Flag-tagged p65 proteins. Immunoprecipitation with an anti-HA antibody was performed.