Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey

Sung Chan Kim, Robert Sprung, Yue Chen, Yingda Xu, Haydn Ball, Jimin Pei, Tzuling Cheng, Yoonjung Kho, Hao Xiao, Lin Xiao, Nick V. Grishin, Michael White, Xiang Jiao Yang, Yingming Zhao

Research output: Contribution to journalArticle

1076 Scopus citations

Abstract

Acetylation of proteins on lysine residues is a dynamic posttranslational modification that is known to play a key role in regulating transcription and other DNA-dependent nuclear processes. However, the extent of this modification in diverse cellular proteins remains largely unknown, presenting a major bottleneck for lysine-acetylation biology. Here we report the first proteomic survey of this modification, identifying 388 acetylation sites in 195 proteins among proteins derived from HeLa cells and mouse liver mitochondria. In addition to regulators of chromatin-based cellular processes, nonnuclear localized proteins with diverse functions were identified. Most strikingly, acetyllysine was found in more than 20% of mitochondrial proteins, including many longevity regulators and metabolism enzymes. Our study reveals previously unappreciated roles for lysine acetylation in the regulation of diverse cellular pathways outside of the nucleus. The combined data sets offer a rich source for further characterization of the contribution of this modification to cellular physiology and human diseases.

Original languageEnglish (US)
Pages (from-to)607-618
Number of pages12
JournalMolecular cell
Volume23
Issue number4
DOIs
StatePublished - Aug 18 2006

Keywords

  • PROTEINS

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., Grishin, N. V., White, M., Yang, X. J., & Zhao, Y. (2006). Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey. Molecular cell, 23(4), 607-618. https://doi.org/10.1016/j.molcel.2006.06.026