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Review
. 2014;13(1):32-41.
doi: 10.4161/cc.27353. Epub 2013 Dec 2.

Protein arginine methylation of non-histone proteins and its role in diseases

Han Wei  1 , Rasika Mundade  1 , Kevin C Lange  2 , Tao Lu  3
Affiliations
Review

Protein arginine methylation of non-histone proteins and its role in diseases

Han Wei et al. Cell Cycle. 2014.

Abstract

Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate arginine residues on histones and other proteins. PRMTs play a crucial role in influencing various cellular functions, including cellular development and tumorigenesis. Arginine methylation by PRMTs is found on both nuclear and cytoplasmic proteins. Recently, there is increasing evidence regarding post-translational modifications of non-histone proteins by PRMTs, illustrating the previously unknown importance of PRMTs in the regulation of various cellular functions by post-translational modifications. In this review, we present the recent developments in the regulation of non-histone proteins by PRMTs.

Keywords: arginine; post-translational modification; protein arginine methyltransferases.

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Figures

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Figure 1. The structure of PRMTs (adapted from ref. 1). All PRMTs universally have 1–2 methyltransferase (MTase) domains. Some have other particular domains. For example, PRMT2 has a SRC homology 3 (SH3) domain. PRMT3 and 9 have zinc finger domains. In addition, PRMT9 also has an F-box domain. PRMT10 has a tetratricopeptide repeat 2 (TPR2) domain. PRMT8 has a unique N-terminal myristoylation (myr) motif.
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Figure 2. Methylation of arginine residues (adapted from ref. 17). Three types of methylated arginine residue products have been proven in mammalian cells. They are ωMMA, ω-aDMA, and ω-sDMA. ωMMA refers to a single methyl group placed on the terminal nitrogen atom. Its production is catalyzed by type I, II, or III PRMTs. ω-aDMA refers to 2 methyl groups placed on the same terminal nitrogen atom. It is catalyzed by type I PRMTs. ω-sDMA refers to 2 methyl groups placed on each of the terminal nitrogens. It is catalyzed by type II PRMTs. δ-MMA so far only has been described in yeast (possibly in plants), and refers to a single methyl group placed on the internal guanidino nitrogen atom. Abbreviations: ω-aDMA, asymmetric ω- NG, NG- dimethylarginines; ωMMA, ω - NG- monomethylarginine; ω-sDMA, symmetric ω - NG, NG- dimethylarginines; δ-MMA, δ-monomethylarginine
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Figure 3. A model of regulation of NFκB by PRMT5 (adopted from ref. 49). In addition to previously known regulatory pathways, NFκB is regulated by PRMT5-mediated methylation of p65 on R30, which affects the expression of many NFκB-induced genes.
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