Arginine methylation catalyzed by PRMT1 is required for B cell activation and differentiation

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作者
Simona Infantino
Amanda Light
Kristy O’Donnell
Vanessa Bryant
Danielle T. Avery
Michael Elliott
Stuart G. Tangye
Gabrielle Belz
Fabienne Mackay
Stephane Richard
David Tarlinton
机构
[1] Walter and Eliza Hall Institute of Medical Research,Department of Medical Biology
[2] University of Melbourne,Department of Immunology and Pathology
[3] Monash University,Immunology Division
[4] Garvan Institute of Medical Research,Sydney Medical School
[5] University of Sydney,Chris O’Brien Lifehouse Cancer Centre
[6] Royal Prince Alfred Hospital,St Vincent’s Clinical School, Faculty of Medicine
[7] University of NSW,Department of Microbiology and Immunology
[8] University of Melbourne,Lady Davis Institute for Medical Research
[9] McGill University,undefined
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Nature Communications | / 8卷
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Arginine methylation catalyzed by protein arginine methyltransferases (PRMT) is a common post-translational modification in mammalian cells, regulating many important functions including cell signalling, proliferation and differentiation. Here we show the role of PRMT1 in B-cell activation and differentiation. PRMT1 expression and activity in human and mouse peripheral B cells increases in response to in vitro or in vivo activation. Deletion of the Prmt1 gene in mature B cells establishes that although the frequency and phenotype of peripheral B cell subsets seem unaffected, immune responses to T-cell-dependent and -independent antigens are substantially reduced. In vitro activation of Prmt1-deficient B cells with a variety of mitogens results in diminished proliferation, differentiation and survival, effects that are correlated with altered signal transduction from the B cell receptor. Thus PRMT1 activity in B cells is required for correct execution of multiple processes that in turn are necessary for humoral immunity.
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  • [1] Bedford MT(2005)Arginine methylation an emerging regulator of protein function Mol. Cell 18 263-272
  • [2] Richard S(2006)Protein arginine methylation in lymphocyte signaling Curr. Opin. Immunol. 18 321-328
  • [3] Blanchet F(2000)Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable Mol. Cell. Biol. 20 4859-4869
  • [4] Schurter BT(2010)Prmt5 is essential for early mouse development and acts in the cytoplasm to maintain ES cell pluripotency Genes Dev. 24 2772-2777
  • [5] Acuto O(2006)Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis Mol. Cell. Biol. 26 3864-3874
  • [6] Pawlak MR(2012)Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor Nucleic Acids Res. 40 9513-9521
  • [7] Scherer CA(2007)Ribosomal protein rpS2 is hypomethylated in PRMT3-deficient mice J. Biol. Chem. 282 16917-16923
  • [8] Chen J(2003)Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice Proc. Natl Acad. Sci. USA 100 6464-6468
  • [9] Roshon MJ(2013)Protein arginine methyltransferases and cancer Nat. Rev. Cancer 13 37-50
  • [10] Ruley HE(2005)CD28 costimulatory signal induces protein arginine methylation in T cells J. Exp. Med. 202 371-377