Brd8, also known as skeletal muscle abundant protein and thyroid hormone receptor coactivating protein of 120 kDa (TrCP120), is a subunit of the NuA4/TIP60-histone acetyltransferase complex. It functions in transcriptional modulation by recognizing acetylated lysine residues on histones and other proteins, and is involved in various biological processes such as cell proliferation, cell cycle progression, and response to cytotoxic agents [2,4]. It is also associated with several diseases, especially cancers [2-4, 10].

In glioblastoma (GBM), BRD8 maintains H2AZ occupancy at p53 target loci through the EP400 histone acetyltransferase complex, leading to a repressive chromatin state that prevents p53 transactivation and sustains proliferation. Targeting BRD8's bromodomain can displace H2AZ, enhance chromatin accessibility, and enforce cell cycle arrest and tumour suppression in TP53 wild-type GBM [1]. In hepatocellular carcinoma (HCC), BRD8, negatively regulated by miR-876-3p, promotes cell proliferation and apoptosis resistance via KAT5 [3]. In colorectal cancer cells, depletion of BRD8 induces cell-cycle arrest at the G1 phase and suppresses cell proliferation by regulating the expression of multiple subunits of the pre-replicative complex [4]. In human lung epithelial cells, depletion of BRD8 increases the secretion of antimicrobial peptide beta-defensin 1 and multiple chemokines, and reduces cell proliferation [5].

In conclusion, Brd8 plays a crucial role in cell-cycle regulation, cell proliferation, and apoptosis in various cancer types. Studies on Brd8 knockout or conditional knockout models have revealed its significance in specific disease areas like glioblastoma, hepatocellular carcinoma, and colorectal cancer. These findings provide potential therapeutic strategies for targeting Brd8 in cancer treatment.