TRIM24 protein, also known as transcriptional intermediary factor 1 alpha (TIF1α), is a multifunctional co-activator protein that interacts dynamically with nuclear receptors and co-activators to influence target gene transcription. This protein belongs to the TRIM family of proteins, which are characterized by a conserved domain structure that includes RING, B-box, and coiled-coil regions. TRIM24 protein interacts with chromatin by recognizing specific histone H3 modifications, showing a high affinity for unmodified lysine 4 (H3K4me0) and acetylated lysine 23 (H3K23ac) of histone H3. This interaction is mediated by its bromodomain, which functions as a "reader" of epigenetic histone marks and regulates chromatin structure and gene expression by connecting relevant proteins to recognized acetylated histone targets. TRIM24 protein is an E3 ubiquitin protein ligase that promotes the proteasomal degradation of p53/TP53 and mediates cell proliferation and apoptosis along with TRIM33. It also regulates the transcriptional activation of retinoic acid (RA) receptors, including RARA, and has been shown to modulate RA-dependent hepatocyte proliferation. In addition, TRIM24 is the first transcription regulatory factor found to have a receptor target located in the nucleus. It can affect the expression and function of proteins related to chromatin remodeling by regulating them. TRIM24 can also utilize retinoic acid (RA) transcription to control tumorigenesis.
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