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

DOI Web Site 71 Citations
  • Chunaram Choudhary
    Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
  • Chanchal Kumar
    Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
  • Florian Gnad
    Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
  • Michael L. Nielsen
    Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
  • Michael Rehman
    Organelle Architecture and Dynamics, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
  • Tobias C. Walther
    Organelle Architecture and Dynamics, Max Planck Institute for Biochemistry, 82152 Martinsried, Germany.
  • Jesper V. Olsen
    Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.
  • Matthias Mann
    Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Martinsried, Germany.

Description

<jats:title>Lysine Acetylation Catalog</jats:title> <jats:p> Covalent posttranslational modification is an essential cellular regulatory mechanism by which the activity of proteins can be controlled. Advances in mass spectrometry made it possible for <jats:bold> Choudhary <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" page="834" related-article-type="in-this-issue" vol="325" xlink:href="10.1126/science.1175371">834</jats:related-article> , published online 16 July) to assess the prevalence of lysine acetylation throughout the whole proteome. Acetylation is much more widespread than previously appreciated and occurs on proteins participating in all sorts of biological functions. Acetylation can influence susceptibility of proteins to phosphorylation and occurs frequently on enzymes that control the modification of other proteins by covalent ubiquitination and on proteins that form large macromolecular complexes. The findings also help to characterize the actions of lysine deacetylase inhibitors, which have shown clinical promise in treatments for cancer. </jats:p>

Journal

  • Science

    Science 325 (5942), 834-840, 2009-08-14

    American Association for the Advancement of Science (AAAS)

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