The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans

Abstract

Information about the family of protein arginine methyltransferases (PRMTs) has been growing rapidly over the last few years and the emerging role of arginine methylation involved in cellular processes like signaling, RNA processing, gene transcription, and cellular transport function has been investigated. To date, 11 PRMTs gene transcripts have been identified in humans. Almost all PRMTs have been shown to have enzymatic activity and to catalyze arginine methylation. This review will summarize the overall function of human PRMTs and include novel highlights on each family member.

Fig. 1

Methylation of the arginine side chain by PRMTs. Depicted is the amino acid arginine in target proteins. Type-I (TypeI) and type-II (TypeII) enzymes catalyze the formation of MMA by transfer of a methyl group to the ω-guanidino group. In addition, transfer of an additional methyl group results in aDMA (type-I enzymes), or sDMA (type-II enzymes). Type-III (TypeIII) enzymes transfer the methyl group to the internal δ-nitrogen

Fig. 2

The human PRMT family. The different members are indicated as boxes and the protein length by the numbers of amino acids. Only the longest isoforms are shown. All PRMTs have at least one conserved Catalytic Domain (shaded gray). Different additional domains are highlighted (green): SH3, ZnF zinc finger, Myr myristoylation, F-box, TPR tetratricopeptide, NosD nitrous oxidase accessory protein

Fig. 3

Phylogenetic analysis of the protein sequences of all PRMTs using guide-tree calculations. The length of the lines indicate the relationship and distance between the PRMT proteins. The sequences for the different PRMTs and the isoforms (indicated by the additional number) are from Table 1