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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Vydáno v:Molecular & cellular oncology Ročník 1; číslo 3; s. e963452
Hlavní autoři: Zhao, Di, Li, Fu-Long, Cheng, Zhou-Li, Lei, Qun-Ying
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States Taylor & Francis 15.09.2014
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ISSN:2372-3556, 2372-3556
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Shrnutí: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.
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ISSN:2372-3556
2372-3556
DOI:10.4161/23723548.2014.963452