The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation.
Post-translational modifications are well-known effectors in DNA damage signaling and epigenetic gene expression. Protein arginine methylation is a covalent modification that results in the addition of methyl groups to the nitrogen atoms of the arginine side chains and is catalyzed by a family of protein arginine methyltransferases (PRMTs). In the past, arginine methylation was mainly observed on abundant proteins such as RNA-binding proteins and histones, but recent advances have revealed a plethora of arginine-methylated proteins implicated in a variety of cellular processes including signal transduction, epigenetic regulation and DNA repair pathways. Herein, we discuss these recent advances, focusing on the role of PRMT1, the major asymmetric arginine methyltransferase, in cellular processes and its link to human diseases.
Nicholson
Thomas B
TB
Novartis Institutes for Biomedical Research, Cambridge, MA 02139, USA.
Chen
Taiping
T
Richard
Stéphane
S
D000818:Animals; D019175:DNA Methylation; D006331:Heart Diseases / Q000201:enzymology* / Q000503:physiopathology*; D006801:Humans; D007674:Kidney Diseases / Q000201:enzymology / Q000503:physiopathology; D008745:Methylation; D009369:Neoplasms / Q000201:enzymology* / Q000503:physiopathology*; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
D012097:Repressor Proteins; C099988:PRMT1 protein, human; D011484:Protein-Arginine N-Methyltransferases