Protein arginine methyltransferase 4 (PRMT4) (PRMT4)

Protein arginine methyltransferase 4 (PRMT4), also known as Coactivator-associated arginine methyltransferase 1 (CARM1), is a Type I arginine methyltransferase that plays a pivotal role in epigenetic regulation by catalyzing the asymmetric dimethylation of arginine residues on histone H3 (specifically R17 and R26) and various non-histone proteins (UniProt Q86X55) [1]. As a transcriptional coactivator, PRMT4 modulates the activity of nuclear receptors and other transcription factors, influencing processes such as cell cycle progression, mRNA splicing, and cellular differentiation (Majumder et al., 2020) [4]. In many human cancers, including breast, prostate, and colorectal carcinomas, PRMT4 is frequently overexpressed or hyperactivated, driving oncogenic programs and promoting tumor cell proliferation and survival (Majumder et al., 2020) [4]. Consequently, PRMT4 has become a high-priority target for small-molecule drug development, with several potent and selective inhibitors like EZM2302 and TP-064 demonstrating preclinical efficacy in reducing tumor growth by blocking its enzymatic activity (Chan-Penebre et al., 2015; Nakayama et al., 2018) [2, 3]. While the prompt specifies PRMT4 mRNA, therapeutic strategies typically focus on inhibiting the functional PRMT4 protein, although RNA-interference techniques (siRNA) and antisense oligonucleotides are widely utilized in preclinical research to validate its role as a target and suppress its expression (Chan-Penebre et al., 2015) [2].

Other names

CARM1Coactivator-associated arginine methyltransferase 1PRMT4

Selective inhibition of the enzymatic activity of Protein arginine methyltransferase 4, thereby preventing the asymmetric dimethylation of arginine residues on histone H3 and non-histone substrates like BAF155 and PABP1 (Chan-Penebre et al., 2015; Nakayama et al., 2018) [2, 3].