Bromodomain adjacent to zinc finger domain protein 2A (BAZ2A)

Bromodomain adjacent to zinc finger domain protein 2A (BAZ2A), also known as TIP5, is a large nuclear protein that serves as the regulatory subunit of the NoRC (nucleolar remodeling complex), a chromatin remodeling complex involved in the transcriptional silencing of ribosomal RNA (rRNA) genes[1][3][4][5][6]. BAZ2A contains both a bromodomain and a plant homeodomain (PHD) type zinc finger, which together recognize and bind specific histone modifications, such as acetylated lysine-16 on histone H4 (H4K16ac)[1][7]. Through these interactions, BAZ2A recruits chromatin-modifying enzymes (like HDAC1 and DNA methyltransferases), leading to heterochromatin formation and the repression of rRNA gene transcription[1]. BAZ2A plays a critical role in establishing and maintaining chromatin architecture, especially in embryonic stem cells, where it regulates the boundary between active and repressive genomic domains to maintain cell function and identity[2]. Loss of BAZ2A alters 3D genome organization, increases chromatin accessibility, and impairs differentiation capacity in pluripotent stem cells[2]. Aberrant expression of BAZ2A, particularly overexpression, has been implicated in promoting cancer cell migration and is associated with poor outcomes in prostate cancer[4]. The bromodomain of BAZ2A is considered a difficult-to-drug target, but structure-based fragment drug discovery campaigns have identified selective inhibitors with low micromolar affinities[4]. BAZ2A has no approved therapeutic drugs, but its role in chromatin regulation, cancer progression, and stem cell biology makes it an attractive target for drug development aimed at cancer and epigenetic diseases[4]. **Note:** Certain entries such as precise drug names, clinically validated safety concerns, or widely accepted biomarkers remain under-investigated or are not yet established in clinical practice as of the current literature[4][1].

Other names

TIP5KIAA0314WALp3TTF-I-interacting protein 5TTF-I interacting peptide 5hWALp3

Inhibition of bromodomain-mediated histone acetyl-lysine recognition; disruption of nucleolar remodeling complex (NoRC) function; interference with transcriptional silencing of rDNA[4]