Global, in vivo, and site-specific phosphorylation dynamics in signaling networks

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Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. / Olsen, Jesper Velgaard; Blagoev, Blagoy; Gnad, Florian; Macek, Boris; Kumar, Chanchal; Mortensen, Peter; Mann, Matthias.

In: Cell, Vol. 127, No. 3, 2006, p. 635-48.

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

Harvard

Olsen, JV, Blagoev, B, Gnad, F, Macek, B, Kumar, C, Mortensen, P & Mann, M 2006, 'Global, in vivo, and site-specific phosphorylation dynamics in signaling networks', Cell, vol. 127, no. 3, pp. 635-48. https://doi.org/10.1016/j.cell.2006.09.026

APA

Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., & Mann, M. (2006). Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell, 127(3), 635-48. https://doi.org/10.1016/j.cell.2006.09.026

Vancouver

Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P et al. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006;127(3):635-48. https://doi.org/10.1016/j.cell.2006.09.026

Author

Olsen, Jesper Velgaard ; Blagoev, Blagoy ; Gnad, Florian ; Macek, Boris ; Kumar, Chanchal ; Mortensen, Peter ; Mann, Matthias. / Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. In: Cell. 2006 ; Vol. 127, No. 3. pp. 635-48.

Bibtex

@article{90ddb1c7caea481aacad71bb4e790eef,
title = "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks",
abstract = "Cell signaling mechanisms often transmit information via posttranslational protein modifications, most importantly reversible protein phosphorylation. Here we develop and apply a general mass spectrometric technology for identification and quantitation of phosphorylation sites as a function of stimulus, time, and subcellular location. We have detected 6,600 phosphorylation sites on 2,244 proteins and have determined their temporal dynamics after stimulating HeLa cells with epidermal growth factor (EGF) and recorded them in the Phosida database. Fourteen percent of phosphorylation sites are modulated at least 2-fold by EGF, and these were classified by their temporal profiles. Surprisingly, a majority of proteins contain multiple phosphorylation sites showing different kinetics, suggesting that they serve as platforms for integrating signals. In addition to protein kinase cascades, the targets of reversible phosphorylation include ubiquitin ligases, guanine nucleotide exchange factors, and at least 46 different transcriptional regulators. The dynamic phosphoproteome provides a missing link in a global, integrative view of cellular regulation.",
author = "Olsen, {Jesper Velgaard} and Blagoy Blagoev and Florian Gnad and Boris Macek and Chanchal Kumar and Peter Mortensen and Matthias Mann",
note = "Keywords: Binding Sites; Databases, Factual; Epidermal Growth Factor; Hela Cells; Humans; Kinetics; Mass Spectrometry; Neoplasm Proteins; Peptides; Phosphorylation; Phosphotyrosine; Protein Binding; Protein Processing, Post-Translational; Proteome; Signal Transduction",
year = "2006",
doi = "10.1016/j.cell.2006.09.026",
language = "English",
volume = "127",
pages = "635--48",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - Global, in vivo, and site-specific phosphorylation dynamics in signaling networks

AU - Olsen, Jesper Velgaard

AU - Blagoev, Blagoy

AU - Gnad, Florian

AU - Macek, Boris

AU - Kumar, Chanchal

AU - Mortensen, Peter

AU - Mann, Matthias

N1 - Keywords: Binding Sites; Databases, Factual; Epidermal Growth Factor; Hela Cells; Humans; Kinetics; Mass Spectrometry; Neoplasm Proteins; Peptides; Phosphorylation; Phosphotyrosine; Protein Binding; Protein Processing, Post-Translational; Proteome; Signal Transduction

PY - 2006

Y1 - 2006

N2 - Cell signaling mechanisms often transmit information via posttranslational protein modifications, most importantly reversible protein phosphorylation. Here we develop and apply a general mass spectrometric technology for identification and quantitation of phosphorylation sites as a function of stimulus, time, and subcellular location. We have detected 6,600 phosphorylation sites on 2,244 proteins and have determined their temporal dynamics after stimulating HeLa cells with epidermal growth factor (EGF) and recorded them in the Phosida database. Fourteen percent of phosphorylation sites are modulated at least 2-fold by EGF, and these were classified by their temporal profiles. Surprisingly, a majority of proteins contain multiple phosphorylation sites showing different kinetics, suggesting that they serve as platforms for integrating signals. In addition to protein kinase cascades, the targets of reversible phosphorylation include ubiquitin ligases, guanine nucleotide exchange factors, and at least 46 different transcriptional regulators. The dynamic phosphoproteome provides a missing link in a global, integrative view of cellular regulation.

AB - Cell signaling mechanisms often transmit information via posttranslational protein modifications, most importantly reversible protein phosphorylation. Here we develop and apply a general mass spectrometric technology for identification and quantitation of phosphorylation sites as a function of stimulus, time, and subcellular location. We have detected 6,600 phosphorylation sites on 2,244 proteins and have determined their temporal dynamics after stimulating HeLa cells with epidermal growth factor (EGF) and recorded them in the Phosida database. Fourteen percent of phosphorylation sites are modulated at least 2-fold by EGF, and these were classified by their temporal profiles. Surprisingly, a majority of proteins contain multiple phosphorylation sites showing different kinetics, suggesting that they serve as platforms for integrating signals. In addition to protein kinase cascades, the targets of reversible phosphorylation include ubiquitin ligases, guanine nucleotide exchange factors, and at least 46 different transcriptional regulators. The dynamic phosphoproteome provides a missing link in a global, integrative view of cellular regulation.

U2 - 10.1016/j.cell.2006.09.026

DO - 10.1016/j.cell.2006.09.026

M3 - Journal article

C2 - 17081983

VL - 127

SP - 635

EP - 648

JO - Cell

JF - Cell

SN - 0092-8674

IS - 3

ER -

ID: 46459793