PRMT2 (E5R1P) Rabbit mAb #67007

Arginine methylation is a prevalent PTM found on both nuclear and cytoplasmic proteins. Arginine methylated proteins are involved in many different cellular processes, including transcriptional regulation, signal transduction, RNA metabolism, and DNA damage repair (1-3). Arginine methylation is carried out by the arginine N-methyltransferase (PRMT) family of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (4). There are three different types of arginine methylation: asymmetric dimethylarginine (aDMA, omega-NG,NG-dimethylarginine), where two methyl groups are placed on one of the terminal nitrogen atoms of the guanidine group of arginine; symmetric dimethylarginine (sDMA, omega-NG,NG-dimethylarginine), where one methyl group is placed on each of the two terminal guanidine nitrogens of arginine; and monomethylarginine (MMA, omega-NG-methylarginine), where a single methyl group is placed on one of the terminal nitrogen atoms of arginine. Each of these modifications has potentially different functional consequences. Though all PRMT proteins catalyze the formation of MMA, Type I PRMTs (PRMT1, 3, 4, 6, and 8) add an additional methyl group to produce aDMA, while Type II PRMTs (PRMT5 and 7) produce sDMA. Methylated arginine residues often reside in glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (5). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within proline-glycine-methionine rich (PGM) motifs (6).

PRMT2 is a Type I PRMT, with an AdoMet binding motif similar to PRMT1 and 3 (7). It directly interacts with PRMT1, enhancing its activity (8). PRMT2 itself is responsible for the H3R8me2a mark, which is a mark of active transcription (9,10). It has been shown to interact with many key regulators, including Rb, NF-κB, ER-alpha, and androgen receptor (11-14). PRMT2 has been shown to be overexpressed in multiple tumor types, including hepatocellular carcinoma and glioblastoma, and its catalytic activity increases tumorigenesis (10,15). Splice variants of PRMT2 have been described in breast cancers and PRMT2 can help regulate alternate splicing through factors such as SAM68. (16-18).