PRMT5 promotes symmetric dimethylation of RNA processing proteins and modulates activated T cell alternative splicing and Ca2+/NFAT signaling Institutional Repository Document uri icon


  • AbstractProtein Arginine Methyltransferase (PRMT) 5 is the major type 2 methyltransferase catalyzing symmetric dimethylation (SDM) of arginine. PRMT5 inhibition or deletion in CD4 Th cells reduces TcR engagement-induced IL-2 production and Th cell expansion and confers protection against experimental autoimmune encephalomyelitis (EAE), the animal model of Multiple Sclerosis. However, the mechanisms by which PRMT5 modulates T helper (Th) cell proliferation are still not completely understood and neither are the methylation targets in T cells. In this manuscript, we uncover the role of PRMT5 on alternative splicing (AS) in activated T cells and identify several targets of PRMT5 SDM involved in splicing. In addition, we find a possible link between PRMT5 mediated AS of Trpm4 (Transient Receptor Potential Cation Channel Subfamily M Member 4) and TcR/NFAT signaling/IL-2 production. This understanding may guide development of drugs targeting these processes to benefit patients with T cell-mediated diseases.

author list (cited authors)

  • Sengupta, S., West, K. O., Sanghvi, S., Laliotis, G., Agosto, L. M., Lynch, K., ... Guerau-de-Arellano, M.

complete list of authors

  • Sengupta, Shouvonik||West, Kelsi O||Sanghvi, Shridhar||Laliotis, Georgios||Agosto, Laura M||Lynch, Kristen||Tsichlis, Philip||Singh, Harpreet||Patrick, Kristin||Guerau-de-Arellano, Mireia

Book Title

  • bioRxiv

publication date

  • August 2021