Impact of acetylation on tumor metabolism

Acetylation of protein lysine residues is a reversible and dynamic process that is controlled by histone acetyltransferases (HATs) and deacetylases (HDACs and SIRTs). Recent studies have revealed that acetylation modulates not only nuclear proteins but also cytoplasmic or mitochondrial proteins, inc...

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Published inMolecular & cellular oncology Vol. 1; no. 3; p. e963452
Main Authors Zhao, Di, Li, Fu-Long, Cheng, Zhou-Li, Lei, Qun-Ying
Format Journal Article
LanguageEnglish
Published United States Taylor & Francis 15.09.2014
Subjects
acetylation
metabolic enzyme
oncogene
Review
tumor metabolism
tumor suppressor
acetylation
metabolic enzyme
tumor suppressor
oncogene
tumor metabolism
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Summary:Acetylation of protein lysine residues is a reversible and dynamic process that is controlled by histone acetyltransferases (HATs) and deacetylases (HDACs and SIRTs). Recent studies have revealed that acetylation modulates not only nuclear proteins but also cytoplasmic or mitochondrial proteins, including many metabolic enzymes. In tumors, cellular metabolism is reprogrammed to provide intermediates for biosynthesis such as nucleotides, fatty acids, and amino acids, and thereby favor the rapid proliferation of cancer cells and tumor development. An increasing number of investigations have indicated that acetylation plays an important role in tumor metabolism. Here, we summarize the substrates that are modified by acetylation, especially oncogenes, tumor suppressor genes, and enzymes that are implicated in tumor metabolism.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:2372-3556
2372-3556
DOI:10.4161/23723548.2014.963452