Journal
SCIENCE
Volume 328, Issue 5981, Pages 1043-1046Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1176495
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Funding
- Canadian Institutes of Health Research [MOP-84314, MOP-57793, MOP-12246]
- Ontario Research Fund [-044]
- National Institutes of Health
- National Center for Research Resources [R01RR024031]
- National Cancer Institute of Canada
- Canada Research Chairs in Functional Genomics and Bioinformatics
- Functional Proteomics
- Lea Reichmann Chair in Cancer Proteomics
- Royal Society
- [CA-126239]
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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.
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