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. 2021 Jul 27;40(37):5613–5625. doi: 10.1038/s41388-021-01961-9

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — a Colocalization of B-Myb and E2F2 protein expression in cell nuclei. HCT116 cells were co-transfected with LV203-B-Myb-Flag and pcDNA3.0-E2F2 expression vector. Forty-eight hours after the transfection, cells were fixed and stained with anti-B-Myb antibody (green) and anti-E2F2 antibody (red). Scale bar 5 μm. b Proximity ligation assays (PLAs) of B-Myb with E2F2 in HCT116 and RKO cells. Red spots are regions of signal amplification. Nuclear stain (Hoechst) is blue. Incubation with either B-Myb or E2F2 antibody alone was used as a control. Scale Bars: 10 μm. c Schematic illustration of the B-Myb and E2F2 structure and deletion mutants. DBD DNA-binding domain, AR acidic region/transactivation domain, CR conserved region, Cyc A Cyclin A/CDK2 binding domain, MB marked box, TAD Transactivation domain. d B-Myb associates with E2F2. HCT116 cells were co-transfected with LV203-B-Myb-Flag and pcDNA3.0-E2F2 expression vector (left panel). HEK293 cells were transiently co-transfected with LV105-Flag-B-Myb or pCDH-puro-HA-E2F2 with the indicated deletion mutants. Forty-eight hours after the transfection, whole cell lysates were prepared and subjected to co-immunoprecipatation assay. e Predicted models of B-Myb-E2F2 protein docking. The 3D homologous structures of B-Myb and E2F2 were searched by online HDOCK server, and the three-dimensional homologous docking models for B-Myb and E2F2 interaction were predicted.