Figure 3
From: USP24 stabilizes bromodomain containing proteins to promote lung cancer malignancy
USP24 interacts with the BRD and stabilizes its protein stability. The H1299 cell lysate was used for IP with anti-USP24 antibody, followed by Western blotting with anti-USP24 and anti-BRD7 antibodies (A). HA-BRD7 (B) or HA-BRG1 (C) was expressed in H1299 cells that were subjected to IP with anti-USP24 antibody, followed by Western blotting with anti-HA and anti-USP24 antibodies. HA-BRD was expressed in H1299 cells that were subjected to IP with anti-USP24 and IgG antibodies; followed by Western blotting with anti-USP24 and anti-HA antibodies (D). H1299 cells and MEFs cells overexpressing myc-Ub and HA-BRD and those in which USP24 had been knocked down were subjected to Western blotting with the indicated antibodies (E). The ubiquitination signal for HA-BRD in H1299 cells following overexpression of myc-Ub and HA-BRD and knockdown of USP24 was determined by IP with anti-HA or anti-myc antibodies, following which Western blotting was carried out with indicated antibodies (F). The interaction between USP24 and the BRD was modeled (G). A structural model of the complex between the catalytic domain of human USP24 (USP24-CD) and the second BRD of human BRD2 (BRD2-BD2) is shown. (G(a)) The USP24-CD molecule is shown as an olive surface and a green cartoon diagram. The BRD2-BD2 molecule is shown as a gray surface and a cyan cartoon diagram. (G(b)) The USP24-CD and BRD-BD2 molecules are shown as spheres. The carbon, nitrogen and oxygen atoms of the USP24-CD molecule are shown in green, black, and magenta, respectively. The carbon atoms, nitrogen atoms and oxygen atoms of the BRD2-BD2 molecule are shown in cyan, blue and red, respectively. Sulfur atoms are shown in gold.
