PRMT8 (E2R7O) Rabbit mAb #83283

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).

PRMT8 is a Type I PRMT closely related to PRMT1 and is expressed primarily in the brain. PRMT8 has a unique N-terminus that is myristoylated, which targets it to the plasma membrane (7). The N-terminal domain also is responsible for PRMT8 activity, and contains two automethylation sites that regulate affinity for AdoMet. (8,9). PRMT8 has been shown to be critical in neural development (10,11). In post-mitotic neurons, PRMT8 provides a protective role against double-stranded DNA breaks that accumulate with aging (12). Overexpression of PRMT8 has been shown to be associated with tau phosphorylation and neuroinflammation (13). PRMT8 is also expressed in stem cells and can control pluripotency and mesodermal fate through the PI3K/Akt/Sox2 axis (14,15).