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  Ultradeep Human Phosphoproteome Reveals a Distinct Regulatory Nature of Tyr and Ser/Thr-Based Signaling

Sharma, K., D'Souza, R. C. J., Tyanova, S., Schaab, C., Wisniewski, J. R., Cox, J., et al. (2014). Ultradeep Human Phosphoproteome Reveals a Distinct Regulatory Nature of Tyr and Ser/Thr-Based Signaling. CELL REPORTS, 8(5), 1583-1594. doi:10.1016/j.celrep.2014.07.036.

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 Creators:
Sharma, Kirti1, Author              
D'Souza, Rochelle C. J.1, Author              
Tyanova, Stefka1, Author              
Schaab, Christoph1, Author              
Wisniewski, Jacek R.1, Author              
Cox, Jürgen1, Author              
Mann, Matthias1, Author              
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1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: SPECTROMETRY-BASED PROTEOMICS; PROTEIN-PHOSPHORYLATION; POSTTRANSLATIONAL MODIFICATIONS; MASS-SPECTROMETRY; TYROSINE PHOSPHORYLATION; SPECIFICITY; CANCER; QUANTIFICATION; PURIFICATION; COMBINATION
 Abstract: Regulatory protein phosphorylation controls normal and pathophysiological signaling in eukaryotic cells. Despite great advances in mass-spectrometry-based proteomics, the extent, localization, and site-specific stoichiometry of this posttranslational modification (PTM) are unknown. Here, we develop a stringent experimental and computational work-flow, capable of mapping more than 50,000 distinct phosphorylated peptides in a single human cancer cell line. We detected more than three-quarters of cellular proteins as phosphoproteins and determined very high stoichiometries in mitosis or growth factor signaling by label-free quantitation. The proportion of phospho-Tyr drastically decreases as coverage of the phosphoproteome increases, whereas Ser/Thr sites saturate only for technical reasons. Tyrosine phosphorylation is maintained at especially low stoichiometric levels in the absence of specific signaling events. Unexpectedly, it is enriched on higher-abundance proteins, and this correlates with the substrate KM values of tyrosine kinases. Our data suggest that P-Tyr should be considered a functionally separate PTM of eukaryotic proteomes.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: CELL REPORTS
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 8 (5) Sequence Number: - Start / End Page: 1583 - 1594 Identifier: ISSN: 2211-1247