RESEARCH

🔊Protein arginine methylation 

Protein arginine methylation is a widespread post-translational modification that plays essential roles in maintaining cellular homeostasis. The methyl group donor for arginine methylation, S-adenosylmethionine (AdoMet), is generated through metabolic pathways such as the folate cycle and polyamine metabolism, linking arginine methylation to cellular metabolic status and nutrient availability.

🔊Protein arginine methyltransferases (PRMTs)

Schematic of arginine methylation reactions. PRMTs catalyze the transfer of methyl groups from S-adenosylmethionine (SAM) to the guanidino group of protein arginine residues. Type I enzymes generate asymmetric dimethylarginine (ADMA), type II enzymes generate symmetric dimethylarginine (SDMA), and type III enzymes catalyze monomethylation (MMA). Nine PRMTs have been identified, each containing conserved motifs important for catalytic activity, including Motif I (VLD/EVGXGXG), Post-I (V/IXG/AXD/E), Motif II (F/I/VDI/L/K), Motif III (LR/KXXG), and the THW loop. PRMTs are classified by enzymatic type (I, II, and III) and show distinct subcellular localization. Although arginine methylation is dynamically regulated in cells, selective arginine demethylases have not yet been clearly identified. Meanwhile, selective PRMT inhibitors have been actively developed, with several currently advancing through clinical trials, highlighting PRMTs as promising therapeutic targets.

🔉Regulation of Cellular Homeostasis by Protein Arginine Methylation

Our laboratory investigates how protein arginine methylation and the non-catalytic functions of arginine methyltransferases (PRMTs) regulate cellular homeostasis. PRMTs are classically recognized as epigenetic writers that methylate histone arginine residues, with H3R2me2a and H3R17me2a playing critical roles in fine-tuning gene expression. Notably, H3R2me2a also serves as a molecular signal for Aurora kinase recruitment to chromosomes during mitosis, highlighting the importance of arginine methylation in cell cycle regulation. Beyond their enzymatic activity, PRMTs function as scaffold proteins that mediate protein–protein interactions, coordinating transcriptional complex assembly, replication stress responses, and cell cycle progression. In addition, arginine methylation and non-catalytic interactions of cytoplasmic substrates regulate mitochondrial dynamics, microtubule organization, autophagy, and cellular energy metabolism. By elucidating both enzyme-dependent and enzyme-independent functions of PRMTs, we aim to understand how dysregulated arginine methylation contributes to human disease and to develop next-generation therapeutic strategies. 

🔉Our research is fully supported by funding from NRF and MSIT

Project No: RS-2025-00563180

• Mid-Career Researcher Grant (Mar 2025 - Feb 2030)

• Title: Dynamic Regulation of Mitochondrial Arginine Methylation: Its Involvement in Doxorubicin-Induced Cardiotoxicity

Project No: RS-2024-00509503

• Korea-EU Global Research Center (Oct 2024 - Dec 2026)

• Title: External Stimulus Responsible Gene Therapy Research Center

Project No: RS-2022-NR070845

• Medical Research Center (Jun 2022 - Feb 2029) 

• Title: Muscle Physiome Research Center
  
  

Project No: RS-2024-00412728 (to Yena Cho)

• NRF PhD Candidate Fellowship (Sep 2024 - Aug 2026)

• Title: The Regulation of Mitochondrial Dynamics through CARM1-DRP1 Axis