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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}

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Dephosphorylation at a Conserved SP Motif Governs cAMP Sensitivity and Nuclear Localization of Class IIa Histone Deacetylases.
D. R. Walkinshaw, R. Weist, L. Xiao, K. Yan, G.-W. Kim, and X.-J. Yang (2013)
J. Biol. Chem. 288, 5591-5605
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Glucose and SIRT2 reciprocally mediate the regulation of keratin 8 by lysine acetylation.
N. T. Snider, J. M. Leonard, R. Kwan, N. W. Griggs, L. Rui, and M. B. Omary (2013)
J. Cell Biol. 200, 241-247
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A Role for Cytoskeletal Protein Acetylation in Modulating Myometrial Activity.
G. N. Europe-Finner, M. J. Taggart, and M. Karolczak-Bayatti (2013)
Reproductive Sciences 20, 175-181
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SIRT3 Weighs Heavily in the Metabolic Balance: A New Role for SIRT3 in Metabolic Syndrome.
M. F. Green and M. D. Hirschey (2013)
J Gerontol A Biol Sci Med Sci 68, 105-107
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Okazaki Fragment Metabolism.
L. Balakrishnan and R. A. Bambara (2013)
Cold Spring Harb Perspect Biol 5, a010173
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Lamin A tail modification by SUMO1 is disrupted by familial partial lipodystrophy-causing mutations.
D. N. Simon, T. Domaradzki, W. A. Hofmann, and K. L. Wilson (2013)
Mol. Biol. Cell 24, 342-350
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Posttranslational Modifications of the Retinoblastoma Tumor Suppressor Protein as Determinants of Function.
J. I. MacDonald and F. A. Dick (2013)
Genes & Cancer
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Hdac6 regulates Tip60-p400 function in stem cells.
P. B. Chen, J.-H. Hung, T. L. Hickman, A. H. Coles, J. F. Carey, Z. Weng, F. Chu, and T. G. Fazzio (2013)
eLife Sci 2, e01557
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PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins.
P. Minguez, I. Letunic, L. Parca, and P. Bork (2013)
Nucleic Acids Res. 41, D306-D311
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Sumoylation of SAE2 C Terminus Regulates SAE Nuclear Localization.
K. Truong, T. D. Lee, B. Li, and Y. Chen (2012)
J. Biol. Chem. 287, 42611-42619
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Mitochondrial Protein Acylation and Intermediary Metabolism: Regulation by Sirtuins and Implications for Metabolic Disease.
J. C. Newman, W. He, and E. Verdin (2012)
J. Biol. Chem. 287, 42436-42443
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Sirtuin Catalysis and Regulation.
J. L. Feldman, K. E. Dittenhafer-Reed, and J. M. Denu (2012)
J. Biol. Chem. 287, 42419-42427
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Human Family with Sequence Similarity 60 Member A (FAM60A) Protein: a New Subunit of the Sin3 Deacetylase Complex.
K. T. Smith, M. E. Sardiu, S. A. Martin-Brown, C. Seidel, A. Mushegian, R. Egidy, L. Florens, M. P. Washburn, and J. L. Workman (2012)
Mol. Cell. Proteomics 11, 1815-1828
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Characterizing Ubiquitination Sites by Peptide-based Immunoaffinity Enrichment.
D. Bustos, C. E. Bakalarski, Y. Yang, J. Peng, and D. S. Kirkpatrick (2012)
Mol. Cell. Proteomics 11, 1529-1540
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