Protein Arginine N Methyltransferase (PRMT) is an enzyme responsible for the transfer of methyl groups from S-adenosyl-l-methionine (SAM) to specific arginine residues in proteins. This methylation plays a crucial role in the regulation of various cellular processes, including gene expression, RNA processing, signal transduction, and protein-protein interactions.
PRMTs are a diverse family of enzymes that can be classified into three main types based on their methylation pattern: type I, type II, and type III. Type I PRMTs catalyze the formation of asymmetric dimethylarginine (ADMA), while type II PRMTs generate symmetric dimethylarginine (SDMA). Type III PRMTs, also known as PRMT7, primarily catalyze monomethylation of arginine residues.
These enzymes are highly conserved across different species and are found in various cellular compartments, including the nucleus, cytoplasm, and mitochondria. They are involved in numerous biological processes, such as chromatin remodeling, RNA metabolism, and signal transduction. Methylation of specific arginine residues by PRMTs can modulate protein-protein interactions, alter protein conformation, and influence protein localization.
Dysregulation of PRMT activity has been associated with various diseases, including cancer, cardiovascular disorders, neurodegenerative diseases, and autoimmune disorders. Consequently, PRMTs have become potential targets for therapeutic interventions. Inhibitors of PRMTs are currently being investigated for their therapeutic potential, particularly in cancer treatment, as they may disrupt the altered protein interactions and signaling pathways that contribute to disease progression.
