PerspectiveCell Biology

Rise of the Rival

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Science  19 Feb 2010:
Vol. 327, Issue 5968, pp. 964-965
DOI: 10.1126/science.1187159

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Like protein phosphorylation, the posttranslational addition of acetyl groups to lysine residues of eukaryotic and prokaryotic proteins has been known for decades (1). The discovery that eukaryotic enzymes implicated in transcriptional regulation can acetylate or deacetylate lysines in chromatin-associated proteins (histones) raised the possibility that dynamic changes in lysine acetylation might provide an important regulatory switch in complex cellular processes (2, 3). A decade ago, Kouzarides made the bold prediction that acetylation might “rival phosphorylation” as a regulator of cell function (4). With proteomics, thousands of mammalian proteins with acetylated lysines have indeed been identified (5, 6), and one of the surprising findings has been that, along with chromatin proteins, metabolic enzymes are highly represented among acetylation substrates. This suggested that changes in acetylation status might alter enzymatic activity to allow the cell to respond to changes in metabolic demands by adjusting flux through critical nodes in the relevant pathways. Reports by Zhao et al. and Wang et al. on pages 1000 and 1004 of this issue, respectively, now validate this hypothesis in the prokaryote Salmonella enterica and in human liver cells (7, 8).