A Global Protein Kinase and Phosphatase Interaction Network in Yeast
Lunenfeld-Tanenbaum Research Institute · University of Michigan · +2 more institutions
Abstract
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…
Citation impact
- FWCI
- 36.61
- Percentile
- 100%
- References
- 23
Authors
20- ABAshton BreitkreutzCorresponding
Lunenfeld-Tanenbaum Research Institute
- HCHyungwon ChoiCorresponding
University of Michigan
- JRJeffrey R. SharomCorresponding
Lunenfeld-Tanenbaum Research Institute, Canada Research Chairs
- LBLorrie BoucherCorresponding
Lunenfeld-Tanenbaum Research Institute
- VNVictor NeduvaCorresponding
Wellcome Centre for Cell Biology
Topics & keywords
- Kinome
- Phosphorylation
- Phosphatase
- Kinase
- Protein phosphorylation
- Biochemistry
- Yeast
- Cell biology