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K(lysine) acetyltransferase 2B (PCAF) is a nuclear enzyme that acts as a histone acetyltransferase, facilitating acetylation of histone and non-histone proteins to regulate chromatin structure and gene expression[1][3][4]. It interacts with transcriptional coactivators p300 and CBP, playing a crucial role in transcriptional activation in response to cellular signals and stress[1][6]. PCAF is involved in various biological processes including cell cycle progression, apoptosis, differentiation, autophagy, and metabolic regulation. Aberrant expression or function of PCAF is implicated in several cancers, particularly hepatocellular carcinoma, where its downregulation is linked to disease progression and poor prognosis[4]. PCAF serves as a coactivator for multiple transcription factors, such as ATF4 and p53, and its acetyltransferase activity can be regulated by autoacetylation and interaction with other epigenetic modifiers[1][6].
Inhibition of acetyltransferase activity (blocks acetylation of histones and non-histone proteins, affecting gene expression and cell fate); Modulation of protein-protein interactions affecting transcriptional regulation
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