Targeting protein arginine methyltransferase 5 in disease

PRMT5 catalyzes the mono-and symmetric dimethylation of the arginine N-guanidine group of a wide variety of target proteins including histones, transcriptional elongation factors, kinases and tumor suppressors by utilizing the essential co-factor S-adenosylmethionine as methyl source. PRMT5 overexpression has been linked to the progression of various diseases, including cancer, and is oftentimes associated with a poor prognosis. Therefore, PRMT5 is promoted as a valuable target for drug discovery approaches and was a subject matter in recent endeavors aiming for the development of specific PRMT5 inhibitors. This review will embrace the significance of PRMT5 as therapeutic target with respect to its molecular inter-dependencies in disease states as well as its implication in drug development approaches.