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Updated: Apr 14, 2026

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
Meeting report on FASEB protein arginine methylation: mechanism to therapeutics
David Shechter1, Rong Huang2, Pooja Shah3
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York, USA.
Abstract:
The inaugural FASEB conference Protein Arginine Methylation: Mechanism to Therapeutics was held in Tsukuba, Japan (January 5-8, 2026), and brought together investigators studying protein arginine methyltransferases (PRMTs) and its methylarginine product. Post-translational arginine methylation, found as monomethylarginine (MMA/Rme1), asymmetric dimethylarginine (ADMA/Rme2a), and symmetric dimethylarginine (SDMA/Rme2s), is increasingly recognized as a central regulator of RNA metabolism, chromatin function, and cellular stress responses. Presentations highlighted emerging directions for the field, including mechanisms linking PRMT activity to RNA processing and gene expression, roles in genome stability, identification of new methylarginine reader proteins, and connections between PRMT function and cellular metabolism. Work on immune and antiviral pathways and neuroscience further expanded the biological scope of PRMT activity. At the same time, significant advances in chemical probes, degraders, and selective inhibitors are enabling more precise interrogation of PRMT biology and accelerating efforts to translate these discoveries into therapeutic strategies.
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