title: A global protein kinase and phosphatase interaction network in yeast.
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 backbone of kinase-kinase interactions cross-connects the proteome and may serve to coordinate diverse cellular responses.
authors.affiliation: Centre for Systems Biology, Samuel Lunenfeld Research Institute, 600 University Avenue, Toronto, Ontario, M5G 1X5, Canada.
authors.forename: Ashton
authors.initials: A
authors.lastname: Breitkreutz
authors.forename: Hyungwon
authors.initials: H
authors.lastname: Choi
authors.forename: Jeffrey R
authors.initials: JR
authors.lastname: Sharom
authors.forename: Lorrie
authors.initials: L
authors.lastname: Boucher
authors.forename: Victor
authors.initials: V
authors.lastname: Neduva
authors.forename: Brett
authors.initials: B
authors.lastname: Larsen
authors.forename: Zhen-Yuan
authors.initials: ZY
authors.lastname: Lin
authors.forename: Bobby-Joe
authors.initials: BJ
authors.lastname: Breitkreutz
authors.forename: Chris
authors.initials: C
authors.lastname: Stark
authors.forename: Guomin
authors.initials: G
authors.lastname: Liu
authors.forename: Jessica
authors.initials: J
authors.lastname: Ahn
authors.forename: Danielle
authors.initials: D
authors.lastname: Dewar-Darch
authors.forename: Teresa
authors.initials: T
authors.lastname: Reguly
authors.forename: Xiaojing
authors.initials: X
authors.lastname: Tang
authors.forename: Ricardo
authors.initials: R
authors.lastname: Almeida
authors.forename: Zhaohui Steve
authors.initials: ZS
authors.lastname: Qin
authors.forename: Tony
authors.initials: T
authors.lastname: Pawson
authors.forename: Anne-Claude
authors.initials: AC
authors.lastname: Gingras
authors.forename: Alexey I
authors.initials: AI
authors.lastname: Nesvizhskii
authors.forename: Mike
authors.initials: M
authors.lastname: Tyers
mesh_terms: D001665:Binding Sites; D002244:Carbon / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000378:metabolism; D004249:DNA Damage; D020935:MAP Kinase Signaling System; D013058:Mass Spectrometry; D053858:Metabolic Networks and Pathways; D008954:Models, Biological; D009584:Nitrogen / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation; D025941:Protein Interaction Mapping; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D021122:Protein Subunits / Q000378:metabolism; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism; D020543:Proteome; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: C074860:CDC14 protein, S cerevisiae; D018797:Cell Cycle Proteins; D021122:Protein Subunits; D020543:Proteome; D029701:Saccharomyces cerevisiae Proteins; D002244:Carbon; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; C500749:target of rapamycin protein, S cerevisiae; D010749:Phosphoprotein Phosphatases; D017027:Protein Tyrosine Phosphatases; D009584:Nitrogen