Sci. Signal., 27 August 2013
Selective Sugar SignalsThe addition of the monosaccharide β-N-acetyl-D-glucosamine (GlcNAc) to serine or threonine residues of proteins through the process of O-GlcNAcylation is a posttranslational modification that can affect protein function (see the Perspective by Hart). Ramakrishnan et al. found that when human T cells were cultured in medium containing a high concentration of glucose, the nuclear factor B (NF-B) subunit c-Rel became O-GlcNAcylated at Ser350. A mutant c-Rel lacking the modifiable serine translocated to the nucleus but was unable to bind to the promoters of genes induced by the T cell receptor, including those encoding the inflammatory cytokines interleukin-2 and interferon-. Together, these data connect sugar metabolism with NF-B function and T cell responses and suggest that targeting the O-GlcNAcylation of c-Rel may be therapeutically beneficial in the treatment of T cell–mediated inflammatory diseases.
Citation: P. Ramakrishnan, P. M. Clark, D. E. Mason, E. C. Peters, L. C. Hsieh-Wilson, D. Baltimore, Activation of the Transcriptional Function of the NF-B Protein c-Rel by O-GlcNAc Glycosylation. Sci. Signal. 6, ra75 (2013).
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