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
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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