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Science 325 (5942): 834-840

Copyright © 2009 by the American Association for the Advancement of Science

Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

Chunaram Choudhary,1,2 Chanchal Kumar,1 Florian Gnad,1 Michael L. Nielsen,1,2 Michael Rehman,3 Tobias C. Walther,3 Jesper V. Olsen,1,2 Matthias Mann1,2,*

Abstract: Lysine acetylation is a reversible posttranslational modification of proteins and plays a key role in regulating gene expression. Technological limitations have so far prevented a global analysis of lysine acetylation’s cellular roles. We used high-resolution mass spectrometry to identify 3600 lysine acetylation sites on 1750 proteins and quantified acetylation changes in response to the deacetylase inhibitors suberoylanilide hydroxamic acid and MS-275. Lysine acetylation preferentially targets large macromolecular complexes involved in diverse cellular processes, such as chromatin remodeling, cell cycle, splicing, nuclear transport, and actin nucleation. Acetylation impaired phosphorylation-dependent interactions of 14-3-3 and regulated the yeast cyclin-dependent kinase Cdc28. Our data demonstrate that the regulatory scope of lysine acetylation is broad and comparable with that of other major posttranslational modifications.

1 Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
2 The Novo Nordisk Foundation Center for Protein Research, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen, Denmark.
3 Organelle Architecture and Dynamics, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.

* To whom correspondence should be addressed. E-mail: mmann{at}biochem.mpg.de

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J. Biol. Chem. 287, 4411-4418
   Abstract »    Full Text »    PDF »
Regulation of Glycolytic Enzyme Phosphoglycerate Mutase-1 by Sirt1 Protein-mediated Deacetylation.
W. C. Hallows, W. Yu, and J. M. Denu (2012)
J. Biol. Chem. 287, 3850-3858
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Conserved Molecular Interactions within the HBO1 Acetyltransferase Complexes Regulate Cell Proliferation.
N. Avvakumov, M.-E. Lalonde, N. Saksouk, E. Paquet, K. C. Glass, A.-J. Landry, Y. Doyon, C. Cayrou, G. A. Robitaille, D. E. Richard, et al. (2012)
Mol. Cell. Biol. 32, 689-703
   Abstract »    Full Text »    PDF »
Histone deacetylases 1 and 2 regulate autophagy flux and skeletal muscle homeostasis in mice.
V. Moresi, M. Carrer, C. E. Grueter, O. F. Rifki, J. M. Shelton, J. A. Richardson, R. Bassel-Duby, and E. N. Olson (2012)
PNAS 109, 1649-1654
   Abstract »    Full Text »    PDF »

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