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. 2018 Feb 6;6(1):16. doi: 10.3390/biomedicines6010016

Figure 2.

Figure 2

Schematic model for the binding of BRD4 to acetylated lysine-310 of RELA/p65 and the role of this interaction in the transcriptional activation of NFκB. Stimulus-dependent acetylation of RELA at lysine-310 by p300 induces the recruitment of BRD4 to the promoter via its bromodomains. BRD4 further activates CDK9 to phosphorylate the CTD (C-terminal domain) of RNA polymerase II and to facilitate the RNA pol II-mediated transcription of NFκB target genes. The p50 factor is a processed form of the REL family member p105 (NFκB1) that heterodimerizes with RELA/p65 and that is required for its transcriptional activation functions.