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. 2024 Aug 30;12:92. doi: 10.1186/s40364-024-00641-6

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Schematic representation of the function of BRD4. In the presence of histone acetyltransferase (CBP/P300), lysine residues on histones are acetylated, and BRD4 binds to acetylated lysine residues and recruits transcription mediators (Mediator), TFs and P-TEFb. Then Ser2 of the RNA polymerase II (RNA Pol II) C-terminal motif (CTM) is phosphorylated via the cycle-dependent kinase 9 (CDK9) in P-TEFb, facilitating the transcription elongation of RNA Pol II. NF-kB consists of P50 and RelA dissociates from IkBα and translocates to the nucleus. Binds to the promoter of the target gene at the NF-kB site. In the presence of P300/CBP, the lysine at position 310 of RelA is acetylated. BRD4 binds to acetylated RelA and recruits P-TEFb. P-TEFb phosphorylates the CTM of RNA Pol II and promotes the transcription of NF-kB-related inflammatory genes