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Published online: 17 March 2010 | doi:10.1038/nchina.2010.33
Metabolism: The role of acetylation in cells
Felix Cheung
Abstract
Protein acetylation regulates cellular metabolism through the modification of enzymes that participate in intermediary metabolism
Original article citation
et al. Regulation of cellular metabolism by protein lysine acetylation. Science 327, 1000–1004 (2010).Introduction

© (2010) istockphoto.com/Sebastian Kaulitzki
Protein acetylation — the introduction of an acetyl group into a protein — is a key regulatory mechanism for transcription in the nucleus, but its function outside the nucleus is largely unknown. Kunliang Guan and Yue Xiong at Fudan University in Shanghai and co-workers1 have now demonstrated that protein acetylation plays a major role in the regulation of cellular metabolism.
The researchers used liquid chromatography and mass spectrometry to analyse purified peptides from the nuclear, mitochondrial and cytosolic fractions of human liver tissues. They identified more than 1,300 acetylated peptides and were able to match them to 1,047 human proteins — 703 of which had not previously been reported to be acetylated.
The researchers compared the acetylated proteins with the liver proteome. They discovered that nearly all intermediary metabolic enzymes — enzymes that participate in glycolysis, gluconeogenesis, the tricarboxylic acid cycle, the urea cycle, fatty acid metabolism and glycogen metabolism — had undergone acetylation.
In cultured human liver cells, changing the concentration of extracellular fuels, such as glucose, amino acids and fatty acids, could alter the abundance of acetylated enzymes. The findings suggest that protein acetylation may play an extensive role in regulation of cellular metabolism in response to extracellular conditions.
As metabolic enzymes in microbes are also known to undergo acetylation (see Metabolism: The role of acetylation in microbes), the researchers believe that protein acetylation is a metabolism-regulating mechanism that is evolutionarily conserved in both eukaryotes and prokaryotes.
The authors of this work are from:
School of Life Sciences, Fudan University, Shanghai, China; Molecular and Cell Biology Lab, Fudan University, Shanghai, China; Center of Proteomics, Institute of Biomedical Sciences, Fudan University, Shanghai, China; Department of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina, USA; Affiliated Zhongshan Hospital, Fudan University, Shanghai, China; Bioinformatics Center, Key Lab of Systems Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China; Medical Research Council, Laboratory of Molecular Biology, Cambridge, UK; Department of Biological Chemistry, Fudan University, Shanghai, China; Department of Pharmacology and Moores Cancer Center, University of California, San Diego, La Jolla, California, USA.
Reference
- Zhao, S. et al. Regulation of cellular metabolism by protein lysine acetylation. Science 327, 1000–1004 (2010). | Article | PubMed | OpenURL | | ChemPort |
