Lysine acetylation targets protein complexes and co-regulates major cellular functions

Chunaram Choudhary, Chanchal Kumar, Florian Gnad, Michael L. Nielsen, Michael Rehman, Tobias C. Walther, Jesper V. Olsen, Matthias Mann

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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.

Original languageEnglish
Pages (from-to)834-840
Number of pages7
JournalScience
Volume325
Issue number5942
DOIs
Publication statusPublished - 2009

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Cite this

Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009). Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science, 325(5942), 834-840. https://doi.org/10.1126/science.1175371