Prmt2, a member of the protein arginine methyltransferase (PRMT) family, is a type I enzyme that catalyzes the arginine methylation of target proteins, producing asymmetric dimethyl arginine. It contains a canonical PRMT methylation core and a unique Src homology 3 domain. Prmt2 is involved in multiple biological processes such as histone methylation, transcriptional regulation, and is associated with pathways like Wnt signaling. It plays a crucial role in various cellular functions and is of great biological importance [2].

In renal cell cancer (RCC), Prmt2 overexpression promotes cell proliferation and motility, and its high expression is correlated with poor clinicopathological characteristics and overall survival. Prmt2-mediated H3R8 asymmetric dimethylation in the WNT5A promoter region enhances WNT5A transcriptional expression, leading to RCC malignant progression [1].

In glioblastomas, Prmt2 is activated by HIF1α under hypoxic conditions, and its inactivation suppresses hypoxia-induced cell migration and tumor progression [3].

In hepatocellular carcinoma (HCC), Prmt2 overexpression is an independent predictor of poor prognosis, and its depletion inhibits cell growth and induces apoptosis. Prmt2 promotes Bcl2 gene expression through H3R8me2a enrichment at the Bcl2 promoter [4].

In acute myeloid leukemia (AML), low PRMT2 expressors show increased inflammatory signatures and inferior survival, and Prmt2 knockout in mouse models leads to increased pro-inflammatory cytokine signaling in macrophages [5].

In conclusion, Prmt2 is involved in multiple biological processes and plays a significant role in various diseases, especially in cancer development. Gene knockout and conditional knockout mouse models have been crucial in revealing its role in specific disease conditions such as RCC, glioblastomas, HCC, and AML, helping us understand its biological functions and providing potential therapeutic targets for these diseases.