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. Author manuscript; available in PMC: 2014 Apr 2.
Published in final edited form as: Cancer Cell. 2012 Oct 16;22(4):506–523. doi: 10.1016/j.ccr.2012.09.003

Figure 4. HDAC3 bridges the interaction between Myc and PRC2 to form a co-repressor complex.

Figure 4

(A) 293T cells were transfected with Myc plasmid or FLAG-HDAC3 plasmid or cotransfected with Myc plasmid and FLAG-HDAC3 plasmid. The whole cell lysates were immunoprecipitated using an antibody against Myc, HDAC3, and control IgG, followed by Western blot with an antibody against Myc, FLAG, SUZ12, and EZH2. (B) Reciprocal Co-IP showing endogenous Co-IP of HDAC3 and SUZ12. Whole cell extracts of Jeko-1 cells were subjected to IP with anti-HDAC3 antibody followed by Western blotting for SUZ12, and similar whole cells extracts were subjected to IP with anti-SUZ12, followed by Western blotting with anti-HDAC3. (C) Co-IP of Myc, HDAC3, and SUZ12/EZH2 in Myc-on and Myc-off P493-6 cells. Cell lysates of P493-6 with and without Tet treatment were immunoprecipitated with Myc, HDAC3, SUZ12, EZH2, and control IgG, respectively, followed by Western blotting with an antibody against Myc, HDAC3, SUZ12, and EZH2. (D) HDAC3-mediated interaction between Myc and SUZ12/EZH2. P493-6 (Myc-on) cells were transfected with HDAC3 siRNA or non-targeting siRNA to knock down HDAC3, and Co-IP experiments were performed to evaluate interaction between Myc and SUZ12/EZH2. A-D, Input is equivalent to 10% of the lysate used for the Co-IP. Results are representative of 3 independent experiments.