Bromodomain-containing protein 3 bromodomain 1 (BRD3-BD1) (BRD3-BD1)

Bromodomain-containing protein 3 bromodomain 1 (BRD3-BD1) is a specific protein module within the BRD3 protein, which belongs to the Bromodomain and Extra-Terminal (BET) family of epigenetic readers [1]. This domain is responsible for recognizing and binding to acetylated lysine residues on histone tails, a key post-translational modification that signals for active gene transcription [2]. By anchoring to chromatin, BRD3-BD1 facilitates the assembly of transcriptional complexes that drive the expression of genes essential for cell growth and survival, such as the MYC oncogene [3]. In clinical contexts, BRD3 is frequently implicated in the pathogenesis of NUT midline carcinoma through chromosomal translocations and is overexpressed in various hematological and solid tumors [4]. Therapeutic strategies targeting BRD3-BD1 involve small-molecule inhibitors that occupy the acetyl-lysine binding pocket, effectively displacing the protein from chromatin and suppressing oncogenic signaling pathways [2, 3]. While promising, the development of these inhibitors faces challenges related to dose-limiting toxicities like thrombocytopenia and the need for greater selectivity between different BET family members and their individual bromodomains [2]. Sources: [1] UniProt Q15059; [2] PubMed 24360278; [3] PubMed 20946927; [4] NCBI Gene ID 8019.

Other names

Bromodomain-containing protein 3RING3-like proteinRING3LORFX

Competitive inhibition of acetylated lysine binding to the bromodomain pocket, leading to displacement of the BET protein from chromatin and subsequent suppression of target gene transcription, particularly the MYC oncogene.