Bromodomain PHD finger transcription factor (BPTF) (BPTF)

Bromodomain PHD finger transcription factor (BPTF) is a critical chromatin-remodeling protein that serves as the largest subunit of the Nucleosome Remodeling Factor (NURF) complex [1.2.2, 1.3.2]. It functions as an epigenetic "reader" by utilizing its bromodomain to recognize acetylated lysine residues, specifically H4K16ac, and its PHD fingers to bind methylated histones such as H3K4me3 [1.3.1, 1.3.2]. These interactions allow BPTF to recruit the NURF complex to specific genomic loci, where it facilitates ATP-dependent nucleosome sliding and regulates the transcription of genes essential for cell proliferation, stem cell maintenance, and the DNA damage response [1.2.2, 1.3.1]. BPTF is frequently overexpressed or amplified in various malignancies, including melanoma, non-small cell lung cancer, and breast cancer, where it drives the expression of oncogenes like c-Myc and promotes tumor progression and chemoresistance [1.2.1, 1.2.2, 1.2.4]. Due to its pivotal role in cancer biology, the BPTF bromodomain has become an attractive therapeutic target, leading to the development of small-molecule inhibitors such as AU1, BZ1, and TP-238 [1.1.1, 1.2.5, 1.4.1]. These inhibitors aim to disrupt BPTF-chromatin interactions, thereby downregulating oncogenic signaling and sensitizing cancer cells to existing therapies [1.1.1, 1.2.3].

Other names

FAC1FALZNURF301Fetal Alzheimer antigen

Inhibition of the BPTF bromodomain prevents its binding to acetylated histones (specifically H4K16ac), which disrupts the recruitment and activity of the NURF chromatin remodeling complex, leading to the downregulation of target oncogenes such as c-Myc [1.2.2, 1.2.5, 1.3.1].