PRMT7

PRMT7 is a unique member of the protein arginine methyltransferase (PRMT) family that catalyzes the ω-monomethylation of arginine residues in a substrate-specific manner^[1][2][3]. Mechanistically, PRMT7 preferentially targets arginine residues within R-X-R motifs flanked by basic amino acids and exhibits optimal enzymatic activity at lower-than-physiological temperatures, distinguishing it from other PRMT isoforms^[1][4]. PRMT7-mediated arginine methylation regulates chromatin structure, RNA splicing, stress response, and cell stemness, thereby influencing gene expression, muscle stem cell physiology, B cell immunity, and neural development^[2][3][5][6]. In disease models, PRMT7 deficiency in mice causes defects in muscle satellite cells and immune cell function, while humans with PRMT7 mutations display intellectual disability, hypotonia, and facial dysmorphisms, highlighting its developmental relevance^[2][3]. Compared with PRMT5 and PRMT9, PRMT7 exclusively produces monomethylarginine, lacks significant symmetric or asymmetric dimethylation, and shows distinct substrate recognition, particularly for histone H2B and R-X-R motifs^[1][4][7]. For experimental applications, selective PRMT7 inhibitors have been developed, enabling modulation of its methyltransferase activity in cellular assays and cancer models, with co-inhibition of PRMT4/5/7 demonstrating synergistic suppression of tumor cell growth^[2][6][8]. Collectively, PRMT7 functions as a context-dependent regulator of arginine methylation with implications for epigenetic regulation, RNA processing, and disease modeling^{[1][2][3][4][6]}.

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