Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

作者：Choudhary Chunaram; Kumar Chanchal; Gnad Florian; Nielsen Michael L; Rehman Michael; Walther Tobias C; Olsen Jesper V; Mann Matthias^*

来源：Science, 2009, 325(5942): 834-840.

DOI：10.1126/science.1175371

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.

• 出版日期2009-8-14