Molecules and Cells

Indexed in /covered by CAS, KoreaScience & DOI/Crossref:eISSN 0219-1032   pISSN 1016-8478

Fig. 1.

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Fig. 1. (A) Amino acid sequence similarities between RUNX1, RUNX2, and RUNX3. Conserved lysines (K) recognized by bromodomain 1 (BD1) of BRD2 are indicated. (B) Schematic of wild-type (BRD2-WT) and mutant BRD2. BD1 interacts with RUNX3 acetylated at K-94 and K-171; BD2 interacts with acetylated histones H4K4-ac, H4K12-ac, and H3K14-ac. Y113 and Y386 are essential tyrosines in BD1 and BD2, respectively. Y > F indicates a tyrosine-to-phenylalanine mutation. (C) HEK293 cells were transfected with Myc-RUNX1, FLAG-BRD2-WT, and FLAG-BRD2 mutant described in Figure 1B. Cells were serum-starved for 24 h, and then stimulated with 10% serum. Cells were harvested 2 h later, and the interactions of the proteins were measured by co-IP and IB, as indicated. (D) HEK293 cells were transfected with Myc-RUNX2, FLAG-BRD2-WT, and FLAG-BRD2 mutant, and then treated as described in Figure 1C. Protein–protein interactions were measured by IP and IB as indicated. (E) HEK293 cells were transfected with Myc-RUNX1, Myc-RUNX2, or Myc-RUNX3; serum-starved for 24 h; and then stimulated with 10% serum. Cells were harvested at the indicated time points, and the levels of the indicated proteins and their time-dependent interactions were measured by co-IP and IB. (F) HEK293 cells were transfected with Myc-KRASG12D with Myc-RUNX1, Myc-RUNX2, or Myc-RUNX3, and treated as described in Figure 1E. The levels of the indicated proteins and their time-dependent interactions were measured by co-IP and IB.
Mol. Cells 2019;42:836~839 https://doi.org/10.14348/molcells.2019.0256
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