Post-translational modification (PTM) is a major mechanism conferring the proteomic diversity. To date, more than 600 types of PTMs have been identified, including phosphorylation, ubiquitination, methylation, and many others. Importantly, targeting the modifiers of PTMs has been proved to be a very successful strategy for cancer treatment. More than 72 kinase inhibitors have been approved by FDA and thousands of inhibitors targeting PTMs are currently being evaluated in clinical trials for various cancers.
Protein arginine methylation is emerging as a common PTM, which is comparable to phosphorylation and ubiquitination. Protein arginine methyltransferases (PRMTs) correspond to “writers” that add methyl group(s) to the arginine in targeted proteins. In contrast, arginine methylation can be reversed by demethylases that function as “erasers” to remove methyl group(s) from arginine. To translate the modifications into biological functions, effector proteins termed “readers” that specifically recognize methylarginine. Studies have demonstrated that protein arginine methylation plays critical roles in various fundamental cellular processes, such as transcription, DNA repair, signal transduction, and immune response.
My laboratory focuses on three research lines.
