@article{ac3ae7b0aa0a11debc73000ea68e967b,
title = "Lysine acetylation targets protein complexes and co-regulates major cellular functions",
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.",
author = "Choudhary, {Chuna Ram} and Chanchal Kumar and Florian Gnad and Nielsen, {Michael L} and Michael Rehman and Walther, {Tobias C} and Olsen, {Jesper V} and Matthias Mann",
note = "Keywords: Acetylation; Amino Acid Motifs; Benzamides; Cell Line, Tumor; Cell Nucleus; Cell Physiological Phenomena; Cytoplasm; Enzyme Inhibitors; Histone Deacetylases; Humans; Hydroxamic Acids; Lysine; Mass Spectrometry; Metabolic Networks and Pathways; Mitochondria; Multiprotein Complexes; Protein Processing, Post-Translational; Protein Structure, Tertiary; Proteins; Proteome; Proteomics; Pyridines; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins",
year = "2009",
doi = "10.1126/science.1175371",
language = "English",
volume = "325",
pages = "834--40",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5942",
}