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


Infantino, S; Light, A; O'Donnell, K; Bryant, V; Avery, DT; ELLIOTT, M; Tangye, SG; Belz, G; Mackay, F; Richard, S; Tarlinton, D
2017-10-12
Naure Communications
Journal Article
8
1
891
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.PRMT1 is an arginine methyltransferase involved in a variety of cell functions. Here the authors delete PRMT1 specifically in mature B cells to show the importance of arginine methylation for B cell proliferation, differentiation and survival, and thereby for humoral immunity.
Springer Nature
Immunology; Molecular Immunology
10.1038/s41467-017-01009-1
29026071
Refer to article for additional funding acknowledgements
Refer to copyright notice on published article.

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Creation Date 2017-10-16 01:59:58 Last Modified 2017-10-16 02:58:46