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Proteome-wide analysis of temporal phosphorylation dynamics in lysophosphatidic acid-induced signaling

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78372

Mäusbacher,  N.
Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78668

Schreiber,  T. B.
Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78611

Schaab,  Christoph
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77883

Daub,  Henrik
Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Mäusbacher, N., Schreiber, T. B., Machatti, M., Schaab, C., & Daub, H. (2012). Proteome-wide analysis of temporal phosphorylation dynamics in lysophosphatidic acid-induced signaling. PROTEOMICS, 12(23-24), 3485-3498. doi:10.1002/pmic.201200172.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-000E-7CC3-D
Zusammenfassung
Most growth factor receptors trigger phosphorylation-based signal transduction to translate environmental stimuli into defined biological responses. In addition to comprehensive and reliable assessment of growth factor-induced phosphoregulation, temporal resolution is needed to gain insights into the organizing principles of the cellular signaling machinery. Here, we introduce a refined experimental design for MS-based phosphoproteomics to reconcile the need for high comprehensiveness and temporal resolution with the key requirement of monitoring biological reproducibility. We treated SILAC-labeled SCC-9 cells with the seven transmembrane receptor ligand lysophosphatidic acid (LPA) and identified more than 17 similar to 000 phosphorylation sites. Filtering for biological replicate quantification yielded five-time point profiles for 6292 site-specific phosphorylations, which we analyzed for statistically significant regulation. Notably, about 30% of these sites changed significantly upon LPA stimulation, indicating extensive phosphoproteome regulation in response to this growth factor. Analysis of time series data identified distinct temporal profiles for different kinase substrate motifs, likely reflecting temporal orchestration of cellular kinase activities. Our data further indicated coordinated regulation of biological processes and phosphoprotein networks upon LPA stimulation. Finally, we detected regulation of functionally characterized phosphorylation sites not yet implicated in LPA signaling, which may foster a better understanding how LPA regulates cellular physiology on the molecular level.