TY - JOUR
T1 - Meeting report on FASEB protein arginine methylation
T2 - mechanism to therapeutics
AU - Shechter, David
AU - Huang, Rong
AU - Shah, Pooja
AU - Dubois, Thierry
AU - Li, Xiao Meng
AU - Parhitko, Andrey
AU - Bedford, Mark T.
AU - Kuang, Shihuan
AU - Chen, Taiping
AU - Yang, Yanzhong
AU - Rajyaguru, Purusharth
AU - Barsyte-Lovejoy, Dalia
AU - Zhao, Xinyang
AU - Xu, Wei
AU - Davies, Clare C.
AU - Tikhanovich, Irina
AU - Tran, Ngoc Tung
AU - Kako, Koichiro
AU - Hashimoto, Misuzu
AU - Luo, Minkui
AU - Hevel, Joan M.
AU - Fukamizu, Akiyoshi
AU - Yu, Michael C.
N1 - Publisher Copyright:
© 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology. This is an open access article under the CC BY license. http://creativecommons.org/licenses/by/4.0/
PY - 2026/6
Y1 - 2026/6
N2 - 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.
AB - 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.
KW - PRMTs
KW - RNA processing
KW - cancer therapeutics
KW - chemical probes
KW - genome stability
KW - methylarginine
KW - methylarginine reader proteins
KW - protein arginine methylation
UR - https://www.scopus.com/pages/publications/105039025491
U2 - 10.1016/j.jbc.2026.111448
DO - 10.1016/j.jbc.2026.111448
M3 - Comment/debate
C2 - 41967639
AN - SCOPUS:105039025491
SN - 0021-9258
VL - 302
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 6
M1 - 111448
ER -