Bromodomain-containing protein 7 (BRD7)

Bromodomain-containing protein 7 (BRD7) is a nuclear transcriptional regulator and epigenetic reader that recognizes acetylated lysine residues on histone H3 and H4 tails via its bromodomain. It is a key component of the PBAF subtype of the SWI/SNF chromatin remodeling complex, participating in transcriptional regulation as both a coactivator (notably of p53) and a corepressor, and is known to activate the Wnt signaling pathway in a DVL1-dependent manner. BRD7 is broadly implicated in cell cycle regulation, tumor suppression (prostate, breast), metabolic regulation (insulin signaling, type 2 diabetes), and male fertility (spermatogenesis). Functional loss or downregulation of BRD7 is associated with tumorigenesis and metabolic dysregulation, and it is being explored as a biomarker and potential therapeutic target in oncology and metabolic disease research. Selective pharmacologic inhibition of BRD7 is an emerging area, but clinical translation is still in preclinical stages, with safety and selectivity against related family members such as BRD9 posing therapeutic challenges.

Other names

BRD7Polybromo-associated BRG1-associated factor complex subunitPBAF complex subunit BRD7

Bromodomain inhibition disrupts acetyl-lysine recognition on histones, modulating chromatin state and downstream gene expression Modulation of transcriptional coactivation or repression roles in target pathways (e.g., p53, Wnt) Enhancement of β-cell survival through VDR-dependent transcription when BRD7 is targeted in combination with VDR ligands and BRD9 inhibitors