Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Logo for

Science 327 (5968): 964-965

Copyright © 2010 by the American Association for the Advancement of Science

Cell Biology

Rise of the Rival

Amanda Norvell1, and Steven B. McMahon2

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).

1 Department of Biology, College of New Jersey, Ewing, NJ 08628, USA.
2 Department of Cancer Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.

E-mail: steven.mcmahon{at}

Quantification of Mitochondrial Acetylation Dynamics Highlights Prominent Sites of Metabolic Regulation.
A. J. Still, B. J. Floyd, A. S. Hebert, C. A. Bingman, J. J. Carson, D. R. Gunderson, B. K. Dolan, P. A. Grimsrud, K. E. Dittenhafer-Reed, D. S. Stapleton, et al. (2013)
J. Biol. Chem. 288, 26209-26219
   Abstract »    Full Text »    PDF »
Sirtuin Catalysis and Regulation.
J. L. Feldman, K. E. Dittenhafer-Reed, and J. M. Denu (2012)
J. Biol. Chem. 287, 42419-42427
   Abstract »    Full Text »    PDF »
Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity.
E. Y. Kim, W. K. Kim, H. J. Kang, J.-H. Kim, S. J. Chung, Y. S. Seo, S. G. Park, S. C. Lee, and K.-H. Bae (2012)
J. Lipid Res. 53, 1864-1876
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882