A Global Protein Kinase and Phosphatase Interaction Network in Yeast
A Global Protein Kinase and Phosphatase Interaction Network in Yeast
Budding Yeast Kinome Revealed Covalent modification of proteins by phosphorylation is a primary means by which cells control the biochemical activities and functions of proteins. To better understand the full spectrum of cellular control mechanisms mediated by phosphorylation, Breitkreutz et al. (p. 1043 ; see the Perspective by Levy et al. ) used mass spectrometry to identify proteins that interacted with the complete set of protein kinases from budding yeast and with other molecules, including phosphatases, which influence phosphorylation reactions. The results reveal a network of interacting protein kinases and phosphatases, and analysis of other interacting proteins suggests previously undiscovered roles for many of these enzymes.
- University of Edinburgh United Kingdom
- University of Michigan–Flint United States
- University of Toronto Canada
- Mount Sinai Hospital Canada
- Lunenfeld-Tanenbaum Research Institute Canada
Binding Sites, Saccharomyces cerevisiae Proteins, Proteome, MAP Kinase Signaling System, Nitrogen, Cell Cycle Proteins, Saccharomyces cerevisiae, Protein Serine-Threonine Kinases, Models, Biological, Carbon, Mass Spectrometry, Protein Subunits, Protein Interaction Mapping, Phosphoprotein Phosphatases, Phosphorylation, Protein Tyrosine Phosphatases, Protein Kinases, Metabolic Networks and Pathways, DNA Damage, Signal Transduction
Binding Sites, Saccharomyces cerevisiae Proteins, Proteome, MAP Kinase Signaling System, Nitrogen, Cell Cycle Proteins, Saccharomyces cerevisiae, Protein Serine-Threonine Kinases, Models, Biological, Carbon, Mass Spectrometry, Protein Subunits, Protein Interaction Mapping, Phosphoprotein Phosphatases, Phosphorylation, Protein Tyrosine Phosphatases, Protein Kinases, Metabolic Networks and Pathways, DNA Damage, Signal Transduction
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