SGD Paper 
Choudhary C, et al. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325(5942):834-40
Abstract: Lysine acetylation is a reversible post-translational modification of proteins with a key role in regulating gene expression. Technological limitations have so far prevented a global analysis of its cellular roles. We used high-resolution mass spectrometry to identify 3,600 lysine acetylation sites on 1,750 proteins and quantified acetylation changes in response to the deacetylase inhibitors SAHA 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 to that of other major post-translational modifications.
| Status: Published | Type: Journal Article | PubMed ID: 19608861 |
Topics addressed in this paper
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
| Topics | Genes linked to topics |
|---|---|
| CDC28 | |
| Mutants/Phenotypes |  |
| Non-Fungal Related Genes/Proteins | |
| Primary Literature | |
| Protein Processing/Modification/Regulation | |
| Strains/Constructs | |
