Abstract
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.
Highlights
Introduction thePRMT2 Protein ArginineArginine methylation is 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 as well as reducing itsH-bonding potential, thereby altering interactions with other proteins or nucleic acids [1,2].Arginine methylation is involved in different cellular processes, including transcriptional regulation, RNA metabolism, DNA repair and signal transduction
It is still unclear whether PRMT2 releases the methylated repressor splicing factor 1 (RSF1) after the enzymatic reaction
It is still unclear whether PRMT2 releases the methylated RSF1 after the enzymatic reaction, limiting its use in enzymology studies
Summary
Arginine methylation is 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. Arginine methylation is involved in different cellular processes, including transcriptional regulation, RNA metabolism, DNA repair and signal transduction (see [2,3] for recent reviews). The nine PRMTs identified in mammals have been classified into three types. I PRMTs, including PRMT1, 2, 3, 4, 6 and 8, catalyze the formation of asymmetric dimethylarginine, while type II PRMTs (PRMT5 and PRMT9) produce symmetric dimethylarginine. This review is focused on PRMT2, one of 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. Recent results in the systematic analysis of PRMT interactomes shed new light on PRMT2 interactants and potential substrates [4]. The interaction of PRMT2 with RNA binding proteins and splicing factors is discussed.
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