Bedford Mark T, Clarke Steven G
The University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, P.O. Box 389, Smithville, TX 78957, USA.
Mol Cell. 2009 Jan 16;33(1):1-13. doi: 10.1016/j.molcel.2008.12.013.
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) works 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.
通过向精氨酸残基添加甲基对蛋白质进行共价标记,可以促进其结合伴侣的识别,或调节其生物学活性。在真核生物中催化此类甲基化反应的一小类基因产物(蛋白质精氨酸甲基转移酶)与不断变化的相关亚基共同作用,以识别不同的细胞底物。这些反应表现出许多可逆共价修饰(如蛋白质磷酸化或蛋白质赖氨酸甲基化)的特征;然而蛋白质精氨酸去甲基化在多大程度上发生尚不清楚。蛋白质精氨酸甲基化在信号转导、mRNA剪接、转录控制、DNA修复和蛋白质转运中已确立了生理作用。