Chapter 293 - Protein Arginine Methylation

Abstract

Posttranslational modification of proteins is a hallmark of signal transduction, allowing cells to alter existing proteins to react rapidly to changes and events in their extracellular environment. Protein phosphorylation on serine, threonine, or tyrosine residues as a mechanism of intracellular signal transduction has been extensively studied. In contrast, the role of protein methylation at lysine, arginine, or histidine residues is much less understood. The subject of this chapter, methylation of arginine residues, was discovered more than 30 years ago, but has only recently received appreciation as a novel mechanism of signal transduction, transcriptional regulation, and protein sorting. As more arginine methylated substrates are discovered, and as novel functions of arginine methylation are reported at a very rapid pace, it appears that this protein modification may be of equal importance to protein phosphorylation in the regulation of cellular functions. This chapter summarizes the current knowledge on protein arginine methyltransferases and the function of arginine methylation in signal transduction. Much additional work is still required to elucidate the regulation of arginine methylation and its role in cellular function. Arginine methylation has just recently begun to be appreciated as a posttranslational modification that contributes significantly to signal transduction, protein sorting. transcriptional regulation, chromatin remodeling, and perhaps disease progression.