Arginine methylation is a ubiquitous and relatively stable post-translational modification (PTM) that occurs in three types: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and symmetric
dimethylarginine (SDMA). Methylarginine marks are catalyzed by members of the protein arginine methyltransferases (PRMTs) family of enzymes. Substrates for arginine methylation are found in most cellular compartments, with RNA-binding proteins forming the majority of PRMT targets. Arginine
methylation often occurs in intrinsically disordered regions of proteins, which impacts biological processes like protein-protein interactions and phase separation, to modulate gene transcription, mRNA splicing and signal transduction. With regards to protein-protein interactions, the major “readers” of methylarginine marks are Tudor domain-containing proteins, although additional domain types and unique protein
folds have also recently been identified as methylarginine readers. Here I will describe the identification and characterization of a new effector protein for methylarginine marks called SART3 and I will also address how the known effector SND1 likely functions as an oncogene.
15/07/2025
Aula A, CU018, 15.00