A Cell-Signaling Network Temporally Resolves Specific versus Promiscuous Phosphorylation
| Autor: | S. Sinan Isik, Louis-Philippe Bergeron-Sandoval, Stephen W. Michnick, Evgeny Kanshin, Pierre Thibault |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Glycerol
Phosphopeptides Proteomics Cell signaling Saccharomyces cerevisiae Biology Microtubules General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Tandem Mass Spectrometry Phosphorylation lcsh:QH301-705.5 Chromatography High Pressure Liquid 030304 developmental biology 0303 health sciences Kinase Osmolar Concentration Phosphoproteomics biology.organism_classification Actins Phosphoric Monoester Hydrolases Cell biology Spindle apparatus Biochemistry lcsh:Biology (General) Signal transduction Protein Kinases 030217 neurology & neurosurgery Signal Transduction |
| Zdroj: | Cell Reports, Vol 10, Iss 7, Pp 1202-1214 (2015) |
| ISSN: | 2211-1247 |
| Popis: | SummaryIf specific and functional kinase- or phosphatase-substrate interactions are optimized for binding compared to promiscuous interactions, then changes in phosphorylation should occur faster on functional versus promiscuous substrates. To test this hypothesis, we designed a high temporal resolution global phosphoproteomics protocol to study the high-osmolarity glycerol (HOG) response in the budding yeast Saccharomyces cerevisiae. The method provides accurate, stimulus-specific measurement of phosphoproteome changes, quantitative analysis of phosphodynamics at sub-minute temporal resolution, and detection of more phosphosites. Rates of evolution of dynamic phosphosites were comparable to those of known functional phosphosites and significantly lower than static or longer-time-frame dynamic phosphosites. Kinetic profile analyses indicated that putatively functional kinase- or phosphatase-substrate interactions occur more rapidly, within 60 s, than promiscuous interactions. Finally, we report many changes in phosphorylation of proteins implicated in cytoskeletal and mitotic spindle dynamics that may underlie regulation of cell cycle and morphogenesis. |
| Databáze: | OpenAIRE |
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