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Front Endocrinol (Lausanne) · Jan 2014
ReviewO-GlcNAcylation, an Epigenetic Mark. Focus on the Histone Code, TET Family Proteins, and Polycomb Group Proteins.
- Vanessa Dehennaut, Dominique Leprince, and Tony Lefebvre.
- Structural and Functional Glycobiology Unit, Lille 1 University , Villeneuve d'Ascq , France ; Institut de Biologie de Lille, Pasteur Institute of Lille, Université Lille Nord de France , Lille , France.
- Front Endocrinol (Lausanne). 2014 Jan 1;5:155.
AbstractThere are increasing evidences that dietary components and metabolic disorders affect gene expression through epigenetic mechanisms. These observations support the notion that epigenetic reprograming-linked nutrition is connected to the etiology of metabolic diseases and cancer. During the last 5 years, accumulating data revealed that the nutrient-sensing O-GlcNAc glycosylation (O-GlcNAcylation) may be pivotal in the modulation of chromatin remodeling and in the regulation of gene expression by being part of the "histone code," and by identifying OGT (O-GlcNAc transferase) as an interacting partner of the TET family proteins of DNA hydroxylases and as a member of the polycomb group proteins. Thus, it is suggested that O-GlcNAcylation is a post-translational modification that links nutrition to epigenetic. This review summarizes recent findings about the interplay between O-GlcNAcylation and the epigenome and enlightens the contribution of the glycosylation to epigenetic reprograming.
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