D Honoria for speaking from Heidelberg engineering in the course of the conduct of the study; and Honoria from ChugaiRoche Ltd., Janssen, Allergan Santen, Roche, and Neurodiem, outside the submitted perform. The remaining authors have no economic relationships relevant to this article to disclose.lifeReviewStructure, Activity and Function on the PRMT2 Protein Arginine MethyltransferaseVincent Cura 1,two,three,four and Jean Cavarelli 1,2,three,4, 1 two 3Institut de G ique et de Biologie Mol ulaire et Cellulaire, 67404 Illkirch, France; [email protected] Centre National de la Recherche Scientifique, UMR 7104, 67404 Illkirch, France Institut National de la Santet de la Recherche M icale, U1258, 67404 Illkirch, France Universitde Strasbourg, 67000 Strasbourg, France Correspondence: [email protected]; Tel.: 33-(0)3-6948-Abstract: PRMT2 belongs towards the protein arginine methyltransferase (PRMT) household, which catalyzes the arginine methylation of target proteins. As a sort I enzyme, PRMT2 produces asymmetric dimethyl arginine and has been shown to possess weak methyltransferase activity on histone substrates in vitro, suggesting that its genuine substrates haven’t but been located. PRMT2 contains the canonical PRMT methylation core as well as a exceptional Src homology three domain. Actinomycin D Cancer research have Shogaol supplier demonstrated its clear implication in many distinct cellular processes. PRMT2 acts as a coactivator of numerous nuclear hormone receptors and is identified to interact using a multitude of splicing-related proteins. In addition, PRMT2 is aberrantly expressed in various cancer types, such as breast cancer and glioblastoma. These reports highlight the crucial part played by PRMT2 as well as the need to have to get a greater characterization of its activity and cellular functions. Key phrases: protein arginine methylation; PRMT2; epigenetics; SH3; cancerCitation: Cura, V.; Cavarelli, J. Structure, Activity and Function in the PRMT2 Protein Arginine Methyltransferase. Life 2021, 11, 1263. ten.3390/life11111263 Academic Editor: Sonia Longhi Received: 20 October 2021 Accepted: 12 November 2021 Published: 19 November1. Introduction Arginine methylation is usually a widespread posttranslational modification in eukaryotes catalyzed by protein arginine methyltransferases (PRMTs), a class of enzymes that transfers methyl groups from S-adenosyl-L-methionine (SAM) to guanidine nitrogen atoms in arginine residues of target proteins. Methylation makes arginine bulkier and more hydrophobic at the same time as lowering its H-bonding possible, thereby altering interactions with other proteins or nucleic acids [1,2]. Arginine methylation is involved in distinct cellular processes, like transcriptional regulation, RNA metabolism, DNA repair and signal transduction (see [2,3] for current reviews). The nine PRMTs identified in mammals have been classified into 3 varieties. Form I PRMTs, which includes PRMT1, two, three, four, six and eight, catalyze the formation of asymmetric dimethylarginine, although sort II PRMTs (PRMT5 and PRMT9) make symmetric dimethylarginine. PRMT7, the only type III PRMT, generates mono-methylarginine. This evaluation is focused on PRMT2, among the least functionally characterized PRMTs. The difficulty in detecting its importance in cellular processes was initially attributed to its low methyl transferase activity on classical PRMT substrates, namely, histone tails. Having said that, numerous research have considering the fact that demonstrated the implication of PRMT2 in transcriptional regulation independently of its catalytic activity and, for that reason, in cancer. In addition, recen.
