Model of possible interactions among ETO, Bcl-6, SMRT/N-CoR, and HDACs. Bcl-6 forms an obligate dimer through its BTB domain, which directly contacts the SMRT corepressor.⁵⁰  The Bcl-6 zinc finger region binds to DNA consensus sites and simultaneously to a central region of ETO. ETO in turn also interacts with SMRT, through its C-terminus (though additional contact sites may exist). SMRT and ETO both recruit HDACs (black circles) to amplify Bcl-6 repression. Undoubtedly, multiple other proteins interact with Bcl-6 and ETO (in white, with question marks) and form a complex repressosome. This model is speculative but is consistent with our data for ETO and SMRT/N-CoR interactions with Bcl-6.