A global protein kinase and phosphatase interaction network in yeast.

Centre for Systems Biology, Samuel Lunenfeld Research Institute, 600 University Avenue, Toronto, Ontario, M5G 1X5, Canada.
The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. The KPI network contained many dense local regions of interactions that suggested new functions. Notably, the cell cycle phosphatase Cdc14 associated with multiple kinases that revealed roles for Cdc14 in mitogen-activated protein kinase signaling, the DNA damage response, and metabolism, whereas interactions of the target of rapamycin complex 1 (TORC1) uncovered new effector kinases in nitrogen and carbon metabolism. An extensive backbone of kinase-kinase interactions cross-connects the proteome and may serve to coordinate diverse cellular responses.
Mesh Terms:
Binding Sites, Carbon, Cell Cycle Proteins, DNA Damage, MAP Kinase Signaling System, Mass Spectrometry, Metabolic Networks and Pathways, Models, Biological, Nitrogen, Phosphoprotein Phosphatases, Phosphorylation, Protein Interaction Mapping, Protein Kinases, Protein Subunits, Protein Tyrosine Phosphatases, Protein-Serine-Threonine Kinases, Proteome, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction
Science May. 21, 2010; 328(5981);1043-6 [PUBMED:20489023]
Download 1912 Interactions For This Publication
101382
Switch View:
  • Interactions (1912)
  • PTM Genes (299)