Protein Arginine Methyltransferase 1 and its Dynamic Regulation Associated with Cellular Processes and Diseases

Post-translational modifications (PTMs) of proteins influence protein degradation, protein- protein interactions, expression of genes, and intracellular signal transduction, thereby regulating major life processes. Among the PTMs occurring within the cytoplasm and nucleus, the most commonly studied one is the arginine methylation of proteins catalyzed by PRMTs. PRMT1 is the most excellent and extensively studied member of the PRMT family. PRMT1 occurs in various isoforms, and the unique sequence splicing of each of these isoforms encodes differential proteins that exhibit different cellular localization, substrate specificity, and enzyme activity. In addition to methylating histones, PRMT1 also methylates a large number of non-histone substrates that regulate a broad range of cellular processes. In recent years, research has revealed an increasing number of pathological diseases caused by the misregulation and aberrant expression of PRMT1, demonstrating the potential of PRMT1 as an effective biomarker for drug targets. In this context, the present study discusses the structural characteristics and the biological functions of PRMT1. Practical Applications: Several diseases originate from aberrant post-translational modifications. The misregulation of the arginine methylation of proteins, which is regulated by PRMTs and influences a series of cellular activities, leads to developmental abnormalities and physiological diseases. PRMT1, which accounts for 85% of the activity of PRMTs, is involved in several cellular processes occurring in various diseases. Multiple inhibitors have been developed and studied for their potential as biomarkers and suitable drug targets in clinical application. The present report summarizes the findings of the most recent studies focusing on the structural characteristics, splicing, substrates, and biological functions of PRMT1, to contribute to future research for deciphering the molecular mechanisms of PRMT1 and drug improvement.