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Reference: Choudhary C, et al. (2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325(5942):834-40

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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.

Reference Type
Journal Article
Authors
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther T, Olsen JV, Mann M
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