Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
Copyright policy )Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
Lysine Acetylation Catalog Covalent posttranslational modification is an essential cellular regulatory mechanism by which the activity of proteins can be controlled. Advances in mass spectrometry made it possible for Choudhary et al. (p. 834 , published online 16 July) to assess the prevalence of lysine acetylation throughout the whole proteome. Acetylation is much more widespread than previously appreciated and occurs on proteins participating in all sorts of biological functions. Acetylation can influence susceptibility of proteins to phosphorylation and occurs frequently on enzymes that control the modification of other proteins by covalent ubiquitination and on proteins that form large macromolecular complexes. The findings also help to characterize the actions of lysine deacetylase inhibitors, which have shown clinical promise in treatments for cancer.
- Max Planck Society Germany
- University of Copenhagen Denmark
- Max Planck Institute of Neurobiology Germany
- University of Turin Italy
- University of Copenhagen Denmark
Cell Nucleus, Cytoplasm, Lysine, Amino Acid Motifs, Proteins, Acetylation, Hydroxamic Acids, Histone Deacetylases, Mass Spectrometry, Cell Physiological Phenomena, Mitochondria, Protein Structure, Tertiary, Histone Deacetylase Inhibitors, Cell Line, Tumor, Multiprotein Complexes, Benzamides, Humans, Enzyme Inhibitors, Protein Processing, Post-Translational, Metabolic Networks and Pathways
Cell Nucleus, Cytoplasm, Lysine, Amino Acid Motifs, Proteins, Acetylation, Hydroxamic Acids, Histone Deacetylases, Mass Spectrometry, Cell Physiological Phenomena, Mitochondria, Protein Structure, Tertiary, Histone Deacetylase Inhibitors, Cell Line, Tumor, Multiprotein Complexes, Benzamides, Humans, Enzyme Inhibitors, Protein Processing, Post-Translational, Metabolic Networks and Pathways
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