Lysine acetylation targets protein complexes and co-regulates major cellular functions.
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.
Mesh Terms:
Acetylation, Amino Acid Motifs, Benzamides, Cell Line, Tumor, Cell Nucleus, Cell Physiological Phenomena, Cytoplasm, Enzyme Inhibitors, Histone Deacetylase 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
Acetylation, Amino Acid Motifs, Benzamides, Cell Line, Tumor, Cell Nucleus, Cell Physiological Phenomena, Cytoplasm, Enzyme Inhibitors, Histone Deacetylase 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
Science
Date: Aug. 14, 2009
PubMed ID: 19608861
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