Abstract
The covalent attachment of β-D-N-acetylglucosamine monosaccharides (O-GlcNAc) to serine/threonine residues of nuclear and cytoplasmic proteins is a major regulatory mechanism in cell physiology. Aberrant O-GlcNAc modification of signaling proteins, metabolic enzymes, and transcriptional and epigenetic regulators has been implicated in cancer. Relentless growth of cancer cells requires metabolic reprogramming that is intertwined with changes in the epigenetic landscape. This review highlights the emerging role of protein O-GlcNAcylation at the interface of cancer metabolism and epigenetics.
Keywords:
Cancer metabolism; Epigenetics; O-GlcNAc; Posttranslational modifications.
Copyright © 2014 Elsevier Ireland Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Acetylglucosamine / metabolism*
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Antigens, Neoplasm / metabolism
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Cell Proliferation
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Energy Metabolism / genetics*
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Epigenesis, Genetic*
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Glycosylation
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Histone Acetyltransferases / metabolism
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Histones / metabolism
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Humans
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Hyaluronoglucosaminidase / metabolism
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N-Acetylglucosaminyltransferases / metabolism
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Neoplasms / genetics*
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Neoplasms / metabolism*
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Protein Processing, Post-Translational / physiology*
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Serine / metabolism
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Signal Transduction / genetics
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Threonine / metabolism
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Transcription Factors / metabolism
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Transcription, Genetic / genetics
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Transcriptional Activation
Substances
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Antigens, Neoplasm
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Histones
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Transcription Factors
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Threonine
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Serine
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Histone Acetyltransferases
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N-Acetylglucosaminyltransferases
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UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase
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OGA protein, human
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Hyaluronoglucosaminidase
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Acetylglucosamine