PRMT7 in cancer: Structure, effects, and therapeutic potentials

Abstract

Protein arginine methyltransferase 7 (PRMT7), a type III methyltransferase responsible solely for arginine mono-methylation, plays a critical role in numerous physiological and pathological processes. Recent studies have highlighted its aberrant expression or mutation in various cancers, implicating it in tumorigenesis, cancer progression, and drug resistance. Consequently, PRMT7 has emerged as a promising target for cancer diagnosis and therapeutic intervention. In this review, we present an overview of the molecular structure of PRMT7, discuss its roles and mechanisms in different cancer types, and analyze the binding modes and structure-activity relationships of reported PRMT7 inhibitors. Furthermore, we identify the challenges encountered in functional exploration and drug development targeting PRMT7, propose potential solutions to these challenges, and outline future directions for the development of PRMT7 inhibitors to inform future drug discovery efforts.