Department of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN 47907, United States.
Curr Protein Pept Sci. 2020;21(7):699-712. doi: 10.2174/1389203721666200507091952.
Protein arginine methyltransferase (PRMT) enzymes play a crucial role in RNA splicing, DNA damage repair, cell signaling, and differentiation. Arginine methylation is a prominent posttransitional modification of histones and various non-histone proteins that can either activate or repress gene expression. The aberrant expression of PRMTs has been linked to multiple abnormalities, notably cancer. Herein, we review a number of non-histone protein substrates for all nine members of human PRMTs and how PRMT-mediated non-histone arginine methylation modulates various diseases. Additionally, we highlight the most recent clinical studies for several PRMT inhibitors.
蛋白质精氨酸甲基转移酶(PRMT)酶在 RNA 剪接、DNA 损伤修复、细胞信号转导和分化中发挥着关键作用。精氨酸甲基化是组蛋白和各种非组蛋白蛋白的一种主要的翻译后修饰,可以激活或抑制基因表达。PRMT 的异常表达与多种异常有关,特别是癌症。本文综述了人类 PRMT 的所有 9 种成员的多种非组蛋白蛋白底物,以及 PRMT 介导的非组蛋白精氨酸甲基化如何调节各种疾病。此外,我们还重点介绍了几种 PRMT 抑制剂的最新临床研究。