4.8 Article

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

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NATURE COMMUNICATIONS
卷 8, 期 -, 页码 -

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NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-01009-1

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  1. National Health and Medical Research Council (NHMRC) Australia program grant [1054925]
  2. DRFG Fellowship
  3. NHMRC Research Fellowship
  4. Australian Research Council Future Fellowship

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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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