Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
Top Cited Papers
- 14 August 2009
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 325 (5942), 834-840
- https://doi.org/10.1126/science.1175371
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.Keywords
This publication has 47 references indexed in Scilit:
- The 14-3-3 proteins: integrators of diverse signaling cues that impact cell fate and cancer developmentTrends in Cell Biology, 2009
- MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantificationNature Biotechnology, 2008
- Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeastNature, 2008
- Lysine Acetylation: Codified Crosstalk with Other Posttranslational ModificationsMolecular Cell, 2008
- The deubiquitinylation and localization of PTEN are regulated by a HAUSP–PML networkNature, 2008
- BAC TransgeneOmics: a high-throughput method for exploration of protein function in mammalsNature Methods, 2008
- Proteomics and genomics: perspectives on drug and target discoveryCurrent Opinion in Chemical Biology, 2008
- HDAC6 Modulates Cell Motility by Altering the Acetylation Level of CortactinMolecular Cell, 2007
- An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone FunctionMolecular Cell, 2007
- Mass spectrometry-based proteomicsNature, 2003