Cura Vincent, Cavarelli Jean
Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France.
Centre National de la Recherche Scientifique, UMR 7104, 67404 Illkirch, France.
Life (Basel). 2021 Nov 19;11(11):1263. doi: 10.3390/life11111263.
PRMT2 belongs to the protein arginine methyltransferase (PRMT) family, which catalyzes the arginine methylation of target proteins. As a type I enzyme, PRMT2 produces asymmetric dimethyl arginine and has been shown to have weak methyltransferase activity on histone substrates in vitro, suggesting that its authentic substrates have not yet been found. PRMT2 contains the canonical PRMT methylation core and a unique Src homology 3 domain. Studies have demonstrated its clear implication in many different cellular processes. PRMT2 acts as a coactivator of several nuclear hormone receptors and is known to interact with a multitude of splicing-related proteins. Furthermore, PRMT2 is aberrantly expressed in several cancer types, including breast cancer and glioblastoma. These reports highlight the crucial role played by PRMT2 and the need for a better characterization of its activity and cellular functions.
PRMT2属于蛋白质精氨酸甲基转移酶（PRMT）家族，该家族催化靶蛋白的精氨酸甲基化。作为一种I型酶，PRMT2产生不对称二甲基精氨酸，并且已表明其在体外对组蛋白底物具有较弱的甲基转移酶活性，这表明尚未找到其真正的底物。PRMT2包含典型的PRMT甲基化核心和一个独特的Src同源3结构域。研究已经证明它在许多不同的细胞过程中具有明确的作用。PRMT2作为几种核激素受体的共激活因子，并且已知与多种剪接相关蛋白相互作用。此外，PRMT2在包括乳腺癌和胶质母细胞瘤在内的几种癌症类型中异常表达。这些报道突出了PRMT2所起的关键作用以及更好地表征其活性和细胞功能的必要性。
