Dupas, T., Lauzier, B. & McGraw, S. O-GlcNAcylation: the sweet side of epigenetics. Epigenetics & Chromatin 16, 49 (2023). https://doi.org/10.1186/s13072-023-00523-5
Dupas, T., Lauzier, B. & McGraw, S. O-GlcNAcylation: the sweet side of epigenetics. Epigenetics & Chromatin 16, 49 (2023). https://doi.org/10.1186/s13072-023-00523-5
Dupas, T., Lauzier, B. & McGraw, S. O-GlcNAcylation: the sweet side of epigenetics. Epigenetics & Chromatin 16, 49 (2023). https://doi.org/10.1186/s13072-023-00523-5
Dupas, T., Lauzier, B. & McGraw, S. O-GlcNAcylation: the sweet side of epigenetics. Epigenetics & Chromatin 16, 49 (2023). https://doi.org/10.1186/s13072-023-00523-5
Abstract
Histones display a wide variety of post-translational modifications, including acetylation, methylation, and phosphorylation. These epigenetic modifications can influence chromatin structure and function without altering the DNA sequence. Histones can also undergo post-translational O-GlcNAcylation, a rather understudied modification that plays critical roles in almost all biological processes and is added and removed by O-linked N-acetylglucosamine transferase and O-GlcNAcase, respectively. This review provides a current overview of our knowledge of how O-GlcNAcylation impacts the histone code both directly and by regulating other chromatin modifying enzymes. This highlights the pivotal emerging role of O-GlcNAcylation as an essential epigenetic marker.
Biology and Life Sciences, Biochemistry and Molecular Biology
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