Protein arginine methyltransferases (PRMTs) are a class of enzymes that catalyze the transfer of methyl groups from S-adenosyl-L-methionine (SAM) to arginine residues in proteins. These enzymes play a crucial role in various cellular processes, including gene expression, RNA processing, signal transduction, and protein-protein interactions.
PRMTs are responsible for the methylation of arginine residues in proteins, leading to the formation of mono- or di-methylated arginine residues. This methylation modifies protein structure and function, influencing protein localization, stability, and protein-protein interactions. Depending on the PRMT isoform and the target protein, arginine methylation can have different effects on protein function, ranging from activating or inhibiting protein activity to influencing protein-protein interactions or signaling pathways.
The PRMT family consists of nine different isoforms divided into three types: type I PRMTs (PRMT1, 2, 3, 4, 6), type II PRMTs (PRMT5, 7), and type III PRMTs (PRMT8, 9). Each isoform has distinct substrate specificities and varying cellular distributions.
Dysregulation of PRMTs has been linked to various diseases, including cancer, cardiovascular diseases, neurological disorders, and autoimmune diseases. Therefore, studying PRMTs and their role in different cellular processes is crucial for understanding disease mechanisms and developing targeted therapies.
In summary, protein arginine methyltransferases (PRMTs) are enzymes that catalyze the methylation of arginine residues in proteins, influencing protein structure, function, and cellular processes.
