Abstract 1594 BRD9 functions as a methylarginine reader to regulate AKT-EZH2 signaling

Arginine methylation has been documented as a ubiquitous PTM and plays important roles in many fundamental cellular processes, including transcription, translation, DNA repair, and signaling transduction. It involves the addition of a methyl group to the guanidino nitrogen atoms of arginine residue by the writers, protein arginine methyltransferases (PRMTs), resulting in three types: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA), and symmetric dimethylarginine (SDMA). Emerged evidence suggests that recognition of methylarginine (Rme) marks by effector proteins (known as readers) is a key mechanism for transducing arginine methylation signals to various cellular processes.