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 1,844 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, while 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.
NOTE: Additional interactions involving these protein kinases and phosphatases have been continually curated at the BioGRID since initial publication. You can access a full set of the latest interaction data for all yeast kinases and phosphatases directly at the BioGRID Yeast Kinome Project