Jun-Dal Kim

TL;DR: This study determined that EWS was physically associated with PRMT8, the novel eighth member of the PRMT family, through the COOH-terminal region of EWS including RGG3 with the NH2- terminal region ofPRMT8 encompassing the S-adenosyl-L-methionine binding domain, and that arginine residues in EWS were asymmetrically dimethylated by PRMT 8 using amino acid analysis with thin-layer chromatography

TL;DR: The structural data indicated that PRMT7 harbors two tandem repeated PRMT core domains that form a novel homodimer‐like structure, and Mutagenesis demonstrated that only the N‐terminal catalytic site ofPRMT7 is responsible for cofactor binding.

TL;DR: It is shown that protein arginine methyltransferase 8 (PRMT8) acts as a phospholipase that directly hydrolyzes PC, generating choline and phosphatidic acid, and suggests that PRMT8 acts both as an arginin methyl transferase and as a PC-hydrolyzing PLD that is essential for proper neurological functions.

TL;DR: It is suggested that p38α participates in the pathogenesis of EAE through IL-17 induction, and positively regulates transcription of the Il17 gene.

TL;DR: It is proposed that leukocytes infiltration via the binding of CRT to ITGAs is necessary for the onset and development of the colitis and the inhibition of this interaction may be a novel therapeutic strategy for the treatment of IBD.