TY - JOUR
T1 - The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation
AU - Nicholson, Thomas B.
AU - Chen, Taiping
AU - Richard, Stéphane
N1 - Funding Information:
This work was supported by grants MOP93811 and MOP67070 from the Canadian Institutes of Health Research.
PY - 2009/12
Y1 - 2009/12
N2 - 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.
AB - 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.
KW - Arginine methylation
KW - DNA damage
KW - Disease
KW - PRMT1
KW - Post-translational modifications
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U2 - 10.1016/j.phrs.2009.07.006
DO - 10.1016/j.phrs.2009.07.006
M3 - Review article
C2 - 19643181
AN - SCOPUS:70350084477
SN - 1043-6618
VL - 60
SP - 466
EP - 474
JO - Pharmacological Research
JF - Pharmacological Research
IS - 6
ER -