Transcriptional adaptor zinc-binding domain 2 (TAZ2), found within CREB-binding protein (CBP) and E1A binding protein p300 (TAZ2)

TAZ2 (Transcriptional adaptor zinc-binding domain 2) is a highly conserved zinc-binding helical domain within the CBP and p300 transcriptional coactivators. It stabilizes its structure using three zinc ions and acts as a promiscuous protein-protein interaction module, binding various transcription factors including p53, E2A, STAT1, p63, and p73 via disorder-to-order transitions of partner peptides[1][5][6]. TAZ2 exhibits autoinhibitory control of the HAT activity of CBP/p300; binding by transcription factors or genetic truncation can relieve its inhibition and activate acetyltransferase function, impacting histone acetylation and downstream transcriptional regulation[4]. Disease mutations leading to TAZ2 truncation are implicated in human cancer, and these cells show heightened vulnerability to histone deacetylase inhibitors, making TAZ2 functionally significant for transcriptional regulation and as a biomarker for therapeutic responsiveness[4].

Other names

CH3 domainTAZ2 domain of CBP/p300

In the context of cancer therapy: sensitization to histone deacetylase inhibition in cells with TAZ2-truncated p300/CBP