Protein arginine methyltransferase 4 (PRMT4)

Protein Arginine Methyltransferase 4 (PRMT4), also commonly known as CARM1, is a type I methyltransferase that catalyzes the asymmetric dimethylation of arginine residues on both histone and non-histone proteins [1, 3, 9]. As a critical transcriptional coactivator, it interacts with nuclear hormone receptors and various transcription factors to promote gene expression, primarily through the modification of histone H3 at arginine residues 17 and 26 [1, 2, 6]. Beyond its epigenetic role, PRMT4 is involved in essential cellular processes such as RNA splicing, mRNA stability, and signal transduction pathways [1, 8]. Dysregulation or overexpression of PRMT4 is strongly associated with the progression of several malignancies, including breast, prostate, and colorectal cancers, as well as acute myeloid leukemia (AML), where it helps maintain an undifferentiated state and promotes cell survival [1, 13, 16, 17]. Because of its central role in oncogenic signaling and gene regulation, PRMT4 has emerged as a promising therapeutic target in oncology [1, 13]. Therapeutic strategies currently focus on small-molecule inhibitors that block its enzymatic activity to restore normal gene expression patterns and inhibit tumor growth [1, 11, 13].

Other names

CARM1Coactivator-associated arginine methyltransferase 1PRMT4Protein arginine N-methyltransferase 4

Inhibition of arginine methyltransferase activity; competitive inhibition of S-adenosylmethionine (SAM) binding; substrate-competitive inhibition