The physiological and pathophysiological role of PRMT1-mediated protein arginine methylation

被引:105
|
作者
Nicholson, Thomas B. [5 ]
Chen, Taiping [5 ]
Richard, Stephane [1 ,2 ,3 ,4 ]
机构
[1] Sir Mortimer B Davis Jewish Hosp, Lady Davis Inst Med Res, Segal Canc Ctr, Bloomfield Ctr Res Aging, Montreal, PQ H3T 1E2, Canada
[2] Sir Mortimer B Davis Jewish Hosp, Terry Fox Mol Oncol Grp, Montreal, PQ H3T 1E2, Canada
[3] McGill Univ, Dept Oncol, Montreal, PQ H3T 1E2, Canada
[4] McGill Univ, Dept Med, Montreal, PQ H3T 1E2, Canada
[5] Novartis Inst Biomed Res, Cambridge, MA 02139 USA
基金
加拿大健康研究院;
关键词
Arginine methylation; Post-translational modifications; PRMT1; Disease; DNA damage; DNA-DAMAGE RESPONSE; ASYMMETRIC DIMETHYLARGININE ADMA; DOUBLE-STRAND BREAKS; NUCLEAR POLY(A)-BINDING PROTEIN; AMYOTROPHIC-LATERAL-SCLEROSIS; ONCOGENE-INDUCED SENESCENCE; NITRIC-OXIDE SYNTHESIS; IN-VIVO; METHYLTRANSFERASE PRMT1; TRANSCRIPTIONAL ACTIVATION;
D O I
10.1016/j.phrs.2009.07.006
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
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. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:466 / 474
页数:9
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