Protein Arginine Methylation in Mammals: Who, What, and Why

By M. Bedford, S. Clarke. Molecules and Cells, 2009

1,757 citations recorded by the source corpus.

The covalent marking of proteins by methyl group addition to arginine residues can promote their recognition by binding partners or can modulate their biological activity. A small family of gene products that catalyze such methylation reactions in eukaryotes (PRMTs) work in conjunction with a changing cast of associated subunits to recognize distinct cellular substrates. These reactions display many of the attributes of reversible covalent modifications such as protein phosphorylation or protein lysine methylation; however, it is unclear to what extent protein arginine demethylation occurs. Physiological roles for protein arginine methylation have been established in signal transduction, mRNA splicing, transcriptional control, DNA repair, and protein translocation.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/82c521f275a5ef4ecb5d6b517d3bb83f081678be

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Citations in the corpus

Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing (2015, background): “Arginine methylation of RNA binding proteins by protein arginine 57 methyltransferases (PRMTs) regulates RNA splicing (Bedford and Clarke, 2009; Bezzi et al., 2013; 58 Cheng et al., 2007; Sinha et al., 2010), subcellular localizations (Matsumoto et al.”
Arginine Methylation: The Coming of Age. (2017, background): “It is carried out by the nine members of the PRMT family (Bedford and Clarke, 2009), although others may exist, such as the putative arginine methyltransferase NDUFAF7 (Zurita Rendón et al., 2014).”
Late Cornified Envelope Group I, a Novel Target of p53, Regulates PRMT5 Activity (2014, background): “Protein arginine methyltransferases (PRMTs) constitute of a large family of enzymes having the arginine methyltransferases activity responsible for catalyzing the formation of monomethyl arginine, asymmetric dimethyl arginine, and symmetric dimethyl arginine (SDMA) [14].”
Regulation of nucleosome dynamics by histone modifications (2013, neutral): “Histones can also be mono-or dimethylated on arginines 33 , but much less is known about the effects of histone arginine methylation on nucleosome dynamics.”
Dysregulation of PRMT1 and PRMT6, Type I arginine methyltransferases, is involved in various types of human cancers (2011, background): “Discussion In recent years, it has become clear that methyl groups stand besides phosphate groups as major controlling elements in protein functions and an arginine residue in proteins is 1 of the most common targets for methylation in mammalian cells.(6,32) Arginine contains 5 potential hydrogen bo”
Defining the RGG/RG motif. (2013, background): “Arginines can either beu-N- monomethylated (MMA), asymmetrically u-N,N-dimethylated arginines (aDMAs), or symmetrically u-NG,N0G-dimethylated arginines (sDMAs) (Bedford and Clarke, 2009).”
PRMT6 increases cytoplasmic localization of p21CDKN1A in cancer cells through arginine methylation and makes more resistant to cytotoxic agents (2015, background): “Since arginine methylation was suggested to regulate the nuclear/cytoplasmic shuttling of proteins [16], we co-introduced p21 and PRMT6 in HeLa cells, and examined subcellular localization of p21.”
GENeration (2015, neutral): “…during both the STAR-100and the ILLIAC IV studies was, Is the preferred configuration to have NASTRAN execute in a host plus "4G" computer ("front-end") environment (e.g. let STARdo what STARdoes best and leave the rest to the CDC6000) of for NASTRANto be completely converted to the "4G" comPuter?”