Authors
Yuchen He, Jiayi Lou, Yijing Huang, Wen Deng, Xuehong Cai
Published in
Oncology reports. Volume 56. Issue 6. Epub Oct 09, 2026.
Abstract
Protein arginine methyltransferase 7 (PRMT7), the sole type III PRMT family member, catalyzes arginine monomethylation and has recently emerged as an important regulator of cancer biology. Increasing evidence indicates that PRMT7 participates in tumor initiation and progression through epigenetic regulation, transcriptional control, RNA processing and signaling pathway modulation. Dysregulated PRMT7 expression has been reported in diverse malignancies, including leukemia, breast cancer, lung cancer, renal cell carcinoma, hepatocellular carcinoma, prostate cancer and gastric cancer. Functionally, PRMT7 has been implicated in epithelial‑mesenchymal transition, cancer stemness, metastasis and immune modulation, although its effects may vary depending on cellular and tumor context. The present review summarizes the structural and biochemical features of PRMT7, its mechanistic roles across different cancer types, and its potential as a therapeutic target. Recent progress in PRMT inhibitor development was also discussed, with particular emphasis on PRMT7‑selective compounds such as SGC3027, SGC8158 and JS1310, as well as the key challenges that remain for clinical translation. Elucidating the context‑specific functions and targetable vulnerabilities of PRMT7 may provide new opportunities for precision cancer therapy.
PMID:
42852627
Bibliographic data and abstract were imported from PubMed on 09 Oct 2026.
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