"Proteins in the bromodomain and extraterminal domain (BET) family, which include BRD2, BRD3, BRD4 and BRDT, play a crucial role in the transcription of RNA polymerase II, a multiprotein complex that travels along DNA and synthesizes RNA as the template. Small-molecule inhibitors that block interactions between BET and acetylated histone proteins have recently been developed as potential targeted therapies for many diseases, including cancer, but have not been successful in clinic."
""Dr. Bin Zheng has made a major discovery in turning the pharmacology of transcriptional regulation through the BET domain protein on its head and is really mechanistically defining what these pathways are to move the field forward,""
"Previous work from the Shilatifard laboratory demonstrated that the BET protein BRD4 does not require bromodomains for its transcriptional elongation function - BET domains recognize and bind to acetylated lysine residues on histones to influence gene expression and DNA repair - to control transcription elongation."
BET family proteins BRD2, BRD3, BRD4 and BRDT play central roles in RNA polymerase II transcription, directing RNA synthesis along DNA. Small-molecule inhibitors that disrupt BET–acetylated histone interactions were developed as targeted therapies for conditions including cancer but failed in clinical application. BRD4 mediates transcriptional elongation without requiring its bromodomains; BET domains recognize acetylated lysine residues on histones to influence gene expression and DNA repair. Identification of mechanisms controlling transcriptional initiation and elongation clarifies how proper gene expression is maintained and suggests paths to improve targeted therapeutic strategies.
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