Prmt7, a member of the protein arginine methyltransferase (PRMT) family, is a type III PRMT that uniquely catalyzes the formation of monomethylarginine [2,3,4]. Protein arginine methylation, a post-translational modification it mediates, is involved in regulating various biological processes such as gene expression, DNA repair, RNA splicing, and stem cell biology [3,4].

Genetic loss of Prmt7 in mouse models has shown several significant findings. In a CML mouse model, targeting Prmt7 delayed leukemia development and impaired self-renewal of leukemia stem cells (LSCs) without affecting normal hematopoiesis. Mechanistically, it reprogramed glycine metabolism by reducing glycine decarboxylase expression, generating methylglyoxal which was detrimental to LSCs [1]. In Prmt7 homozygous knockout mice, defects were found in muscle stem cells and immune cells [3]. In cardiac-specific Prmt7 ablation (cKO) mice, male cKO mice showed impaired cardiac function, myocardial hypertrophy, and interstitial fibrosis, while female cKO mice showed similar phenotypes mainly after menopause or ovariectomy. Prmt7 was found to regulate the JAK/STAT/Socs3 signaling pathway [5].

In conclusion, Prmt7 is crucial for multiple biological processes. Through gene knockout mouse models, its role in diseases like CML and post-menopausal cardiomyopathy has been revealed. These models have provided valuable insights into how Prmt7 functions in specific biological processes and disease conditions, highlighting its potential as a therapeutic target.