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

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 diffe...

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Detalles Bibliográficos
Autores principales: Infantino, Simona, Light, Amanda, O’Donnell, Kristy, Bryant, Vanessa, Avery, Danielle T., Elliott, Michael, Tangye, Stuart G., Belz, Gabrielle, Mackay, Fabienne, Richard, Stephane, Tarlinton, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5638811/
https://www.ncbi.nlm.nih.gov/pubmed/29026071
http://dx.doi.org/10.1038/s41467-017-01009-1
Descripción
Sumario: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.