Lysine acetylation targets protein complexes and co-regulates major cellular functions

Research output: Contribution to journal › Journal article › peer-review

Standard

Lysine acetylation targets protein complexes and co-regulates major cellular functions. / Choudhary, Chuna Ram; Kumar, Chanchal; Gnad, Florian; Nielsen, Michael L; Rehman, Michael; Walther, Tobias C; Olsen, Jesper V; Mann, Matthias.

In: Science, Vol. 325, No. 5942, 2009, p. 834-40.

Research output: Contribution to journal › Journal article › peer-review

Harvard

Choudhary, CR, Kumar, C, Gnad, F, Nielsen, ML, Rehman, M, Walther, TC, Olsen, JV & Mann, M 2009, 'Lysine acetylation targets protein complexes and co-regulates major cellular functions', Science, vol. 325, no. 5942, pp. 834-40. https://doi.org/10.1126/science.1175371

APA

Choudhary, C. R., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009). Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science, 325(5942), 834-40. https://doi.org/10.1126/science.1175371

Vancouver

Choudhary CR, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009;325(5942):834-40. https://doi.org/10.1126/science.1175371

Author

Choudhary, Chuna Ram ; Kumar, Chanchal ; Gnad, Florian ; Nielsen, Michael L ; Rehman, Michael ; Walther, Tobias C ; Olsen, Jesper V ; Mann, Matthias. / Lysine acetylation targets protein complexes and co-regulates major cellular functions. In: Science. 2009 ; Vol. 325, No. 5942. pp. 834-40.

Bibtex

@article{ac3ae7b0aa0a11debc73000ea68e967b,
title = "Lysine acetylation targets protein complexes and co-regulates major cellular functions",
abstract = "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.",
author = "Choudhary, {Chuna Ram} and Chanchal Kumar and Florian Gnad and Nielsen, {Michael L} and Michael Rehman and Walther, {Tobias C} and Olsen, {Jesper V} and Matthias Mann",
note = "Keywords: Acetylation; Amino Acid Motifs; Benzamides; Cell Line, Tumor; Cell Nucleus; Cell Physiological Phenomena; Cytoplasm; Enzyme Inhibitors; Histone Deacetylases; Humans; Hydroxamic Acids; Lysine; Mass Spectrometry; Metabolic Networks and Pathways; Mitochondria; Multiprotein Complexes; Protein Processing, Post-Translational; Protein Structure, Tertiary; Proteins; Proteome; Proteomics; Pyridines; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins",
year = "2009",
doi = "10.1126/science.1175371",
language = "English",
volume = "325",
pages = "834--40",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5942",

}

RIS

TY - JOUR

T1 - Lysine acetylation targets protein complexes and co-regulates major cellular functions

AU - Choudhary, Chuna Ram

AU - Kumar, Chanchal

AU - Gnad, Florian

AU - Nielsen, Michael L

AU - Rehman, Michael

AU - Walther, Tobias C

AU - Olsen, Jesper V

AU - Mann, Matthias

N1 - Keywords: Acetylation; Amino Acid Motifs; Benzamides; Cell Line, Tumor; Cell Nucleus; Cell Physiological Phenomena; Cytoplasm; Enzyme Inhibitors; Histone Deacetylases; Humans; Hydroxamic Acids; Lysine; Mass Spectrometry; Metabolic Networks and Pathways; Mitochondria; Multiprotein Complexes; Protein Processing, Post-Translational; Protein Structure, Tertiary; Proteins; Proteome; Proteomics; Pyridines; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

U2 - 10.1126/science.1175371

DO - 10.1126/science.1175371

M3 - Journal article

C2 - 19608861

VL - 325

SP - 834

EP - 840

JO - Science

JF - Science

SN - 0036-8075

IS - 5942

ER -

ID: 14701277