Interleukin enhancer-binding factor 2 (ILF2) (ILF2)

Interleukin enhancer-binding factor 2 (ILF2), also known as NF45, is a 45 kDa nuclear protein that serves as a critical regulator of gene expression, RNA metabolism, and genomic stability. It primarily functions as a heterodimer with ILF3 (NF90), forming a complex that binds to both DNA and RNA to modulate transcription, mRNA splicing, and translation. Originally identified as a component of the nuclear factor of activated T-cells (NFAT) complex required for interleukin-2 expression in T cells, ILF2 is now recognized as a potent oncogene in various malignancies, including multiple myeloma, hepatocellular carcinoma, and non-small cell lung cancer. Its overexpression, frequently driven by 1q21.3 chromosomal amplification, promotes tumor cell proliferation, inhibits apoptosis, and confers resistance to DNA-damaging agents by enhancing DNA repair mechanisms and R-loop resolution. Emerging therapeutic approaches include the development of small-molecule inhibitors like NYH002, which targets the ILF2-DHX9 interaction to disrupt R-loop resolution and induce selective cytotoxicity in cancer cells.

Other names

NF45Nuclear factor of activated T-cells 45 kDaPRO3063Interleukin enhancer-binding factor 2, 45kDaNFAT45

Inhibition of ILF2-mediated transcriptional regulation and RNA processing; disruption of the ILF2-DHX9 interaction to impair R-loop resolution and induce DNA damage-mediated apoptosis in cancer cells.