Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle

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Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. / Daub, Henrik; Olsen, Jesper V; Bairlein, Michaela; Gnad, Florian; Oppermann, Felix S; Körner, Roman; Greff, Zoltán; Kéri, György; Stemmann, Olaf; Mann, Matthias.

In: Molecular Cell, Vol. 31, No. 3, 2008, p. 438-48.

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

Harvard

Daub, H, Olsen, JV, Bairlein, M, Gnad, F, Oppermann, FS, Körner, R, Greff, Z, Kéri, G, Stemmann, O & Mann, M 2008, 'Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle', Molecular Cell, vol. 31, no. 3, pp. 438-48. https://doi.org/10.1016/j.molcel.2008.07.007

APA

Daub, H., Olsen, J. V., Bairlein, M., Gnad, F., Oppermann, F. S., Körner, R., Greff, Z., Kéri, G., Stemmann, O., & Mann, M. (2008). Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Molecular Cell, 31(3), 438-48. https://doi.org/10.1016/j.molcel.2008.07.007

Vancouver

Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Körner R et al. Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Molecular Cell. 2008;31(3):438-48. https://doi.org/10.1016/j.molcel.2008.07.007

Author

Daub, Henrik ; Olsen, Jesper V ; Bairlein, Michaela ; Gnad, Florian ; Oppermann, Felix S ; Körner, Roman ; Greff, Zoltán ; Kéri, György ; Stemmann, Olaf ; Mann, Matthias. / Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. In: Molecular Cell. 2008 ; Vol. 31, No. 3. pp. 438-48.

Bibtex

@article{50919390aa1011debc73000ea68e967b,
title = "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle",
abstract = "Protein kinases are pivotal regulators of cell signaling that modulate each other's functions and activities through site-specific phosphorylation events. These key regulatory modifications have not been studied comprehensively, because low cellular abundance of kinases has resulted in their underrepresentation in previous phosphoproteome studies. Here, we combine kinase-selective affinity purification with quantitative mass spectrometry to analyze the cell-cycle regulation of protein kinases. This proteomics approach enabled us to quantify 219 protein kinases from S and M phase-arrested human cancer cells. We identified more than 1000 phosphorylation sites on protein kinases. Intriguingly, half of all kinase phosphopeptides were upregulated in mitosis. Our data reveal numerous unknown M phase-induced phosphorylation sites on kinases with established mitotic functions. We also find potential phosphorylation networks involving many protein kinases not previously implicated in mitotic progression. These results provide a vastly extended knowledge base for functional studies on kinases and their regulation through site-specific phosphorylation.",
author = "Henrik Daub and Olsen, {Jesper V} and Michaela Bairlein and Florian Gnad and Oppermann, {Felix S} and Roman K{\"o}rner and Zolt{\'a}n Greff and Gy{\"o}rgy K{\'e}ri and Olaf Stemmann and Matthias Mann",
note = "Keywords: Amino Acid Sequence; Cell Cycle; Enzyme Activation; Hela Cells; Humans; Mitosis; Molecular Sequence Data; Phosphopeptides; Phosphoproteins; Phosphorylation; Phosphotransferases; Proteomics; S Phase; Substrate Specificity",
year = "2008",
doi = "10.1016/j.molcel.2008.07.007",
language = "English",
volume = "31",
pages = "438--48",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle

AU - Daub, Henrik

AU - Olsen, Jesper V

AU - Bairlein, Michaela

AU - Gnad, Florian

AU - Oppermann, Felix S

AU - Körner, Roman

AU - Greff, Zoltán

AU - Kéri, György

AU - Stemmann, Olaf

AU - Mann, Matthias

N1 - Keywords: Amino Acid Sequence; Cell Cycle; Enzyme Activation; Hela Cells; Humans; Mitosis; Molecular Sequence Data; Phosphopeptides; Phosphoproteins; Phosphorylation; Phosphotransferases; Proteomics; S Phase; Substrate Specificity

PY - 2008

Y1 - 2008

N2 - Protein kinases are pivotal regulators of cell signaling that modulate each other's functions and activities through site-specific phosphorylation events. These key regulatory modifications have not been studied comprehensively, because low cellular abundance of kinases has resulted in their underrepresentation in previous phosphoproteome studies. Here, we combine kinase-selective affinity purification with quantitative mass spectrometry to analyze the cell-cycle regulation of protein kinases. This proteomics approach enabled us to quantify 219 protein kinases from S and M phase-arrested human cancer cells. We identified more than 1000 phosphorylation sites on protein kinases. Intriguingly, half of all kinase phosphopeptides were upregulated in mitosis. Our data reveal numerous unknown M phase-induced phosphorylation sites on kinases with established mitotic functions. We also find potential phosphorylation networks involving many protein kinases not previously implicated in mitotic progression. These results provide a vastly extended knowledge base for functional studies on kinases and their regulation through site-specific phosphorylation.

AB - Protein kinases are pivotal regulators of cell signaling that modulate each other's functions and activities through site-specific phosphorylation events. These key regulatory modifications have not been studied comprehensively, because low cellular abundance of kinases has resulted in their underrepresentation in previous phosphoproteome studies. Here, we combine kinase-selective affinity purification with quantitative mass spectrometry to analyze the cell-cycle regulation of protein kinases. This proteomics approach enabled us to quantify 219 protein kinases from S and M phase-arrested human cancer cells. We identified more than 1000 phosphorylation sites on protein kinases. Intriguingly, half of all kinase phosphopeptides were upregulated in mitosis. Our data reveal numerous unknown M phase-induced phosphorylation sites on kinases with established mitotic functions. We also find potential phosphorylation networks involving many protein kinases not previously implicated in mitotic progression. These results provide a vastly extended knowledge base for functional studies on kinases and their regulation through site-specific phosphorylation.

U2 - 10.1016/j.molcel.2008.07.007

DO - 10.1016/j.molcel.2008.07.007

M3 - Journal article

C2 - 18691976

VL - 31

SP - 438

EP - 448

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 3

ER -

ID: 14701449