2000
The Effects of Changing the Site of Activating Phosphorylation in CDK2 from Threonine to Serine*
Kaldis P, Cheng A, Solomon M. The Effects of Changing the Site of Activating Phosphorylation in CDK2 from Threonine to Serine*. Journal Of Biological Chemistry 2000, 275: 32578-32584. PMID: 10931829, DOI: 10.1074/jbc.m003212200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionCDC2-CDC28 KinasesCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesHumansKineticsMutagenesis, Site-DirectedPhosphorylationProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRecombinant ProteinsSerineSubstrate SpecificityThreonineConceptsWild-type Cdk2Cyclin-dependent kinasesThreonine residuesRNA polymerase IIDegradation of cyclinsHeLa cell extractsCell cycle progressionEssential phosphorylationHuman CDK2Efficient phosphorylationActivating PhosphorylationPolymerase IICyclin HTerminal domainHistone H1Cycle progressionCell extractsPhosphorylationCyclinCDK2General defectCAKKinaseSerineThreonineAnalysis of CAK activities from human cells
Kaldis P, Solomon M. Analysis of CAK activities from human cells. The FEBS Journal 2000, 267: 4213-4221. PMID: 10866826, DOI: 10.1046/j.1432-1327.2000.01455.x.Peer-Reviewed Original ResearchConceptsCdk-activating kinaseCAK activityHuman cellsTranscription factor IIHRNA polymerase IICyclin-dependent kinasesCell cycle progressionPolymerase IIThreonine residuesLarge subunitCyclin HTerminal domainSubstrate specificityCak1pKinase activityMonomeric enzymeMO15HeLa cellsATP analogKinaseSubunitsActivating Phosphorylation of the Saccharomyces cerevisiae Cyclin-dependent Kinase, Cdc28p, Precedes Cyclin Binding
Ross K, Kaldis P, Solomon M. Activating Phosphorylation of the Saccharomyces cerevisiae Cyclin-dependent Kinase, Cdc28p, Precedes Cyclin Binding. Molecular Biology Of The Cell 2000, 11: 1597-1609. PMID: 10793138, PMCID: PMC14870, DOI: 10.1091/mbc.11.5.1597.Peer-Reviewed Original ResearchMeSH KeywordsAntibody SpecificityCDC28 Protein Kinase, S cerevisiaeCell CycleCyclin ACyclin BCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsEnzyme ActivationEpitopesMutationPhosphorylationProtein Serine-Threonine KinasesRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThreonineConceptsCyclin bindingCyclin-dependent kinasesEukaryotic cell cycle progressionConserved threonine residueAddition of cyclinCell cycle progressionHigher eukaryotesThreonine residuesCdc28pCDK activationProtein kinaseRegulatory mechanismsCycle progressionCell cycleCyclinKinasePhosphorylationCak1pActivation pathwayCDKBindingEukaryotesActivationMutantsThreonine
1999
Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
Cheng A, Ross K, Kaldis P, Solomon M. Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes & Development 1999, 13: 2946-2957. PMID: 10580002, PMCID: PMC317162, DOI: 10.1101/gad.13.22.2946.Peer-Reviewed Original ResearchMeSH KeywordsCDC28 Protein Kinase, S cerevisiaeCell CycleCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesEnzyme ActivationFungal ProteinsGene Expression Regulation, FungalHumansPhosphoprotein PhosphatasesPhosphorylationPhosphothreonineProtein Phosphatase 2Protein Phosphatase 2CProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityConceptsCyclin-dependent protein kinasesProtein phosphataseYeast cyclin-dependent protein kinaseType 2C protein phosphatasesType 2C proteinPhosphatase activityHeLa cell extractsCyclin-dependent kinasesCell cycle progressionHuman CDK2Growth defectPredominant phosphatasesProtein kinaseSubstrate specificityKinase activitySynthetic lethalityCycle progressionCell extractsKinasePP2CDephosphorylationPhosphorylationPhosphatasePTC2Ptc2p
1998
Human and Yeast Cdk-activating Kinases (CAKs) Display Distinct Substrate Specificities
Kaldis P, Russo A, Chou H, Pavletich N, Solomon M. Human and Yeast Cdk-activating Kinases (CAKs) Display Distinct Substrate Specificities. Molecular Biology Of The Cell 1998, 9: 2545-2560. PMID: 9725911, PMCID: PMC25525, DOI: 10.1091/mbc.9.9.2545.Peer-Reviewed Original ResearchConceptsTranscription factor IIHC-terminal domainSubstrate specificityCDK/cyclin complexesCTD kinase activityRNA polymerase IIDistinct substrate specificitiesDifferent substrate specificitiesCyclin-dependent kinasesCell cycle progressionHuman CAKYeast CdkEnzyme-substrate recognitionPolymerase IILarge subunitTranscriptional componentsCak1pCDK activationCyclin complexesKey residuesKinase activitySingle polypeptideCycle progressionCDK inhibitorsCDK
1996
The Cdk-Activating Kinase (CAK) from Budding Yeast
Kaldis P, Sutton A, Solomon M. The Cdk-Activating Kinase (CAK) from Budding Yeast. Cell 1996, 86: 553-564. PMID: 8752210, DOI: 10.1016/s0092-8674(00)80129-4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCDC28 Protein Kinase, S cerevisiaeCDC2-CDC28 KinasesCell CycleCell Cycle ProteinsCyclin BCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsFungal ProteinsGenes, FungalMolecular Sequence DataMolecular WeightPhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidStructure-Activity RelationshipConceptsCDK-Activating KinaseBasal transcription factorsTemperature-sensitive mutationProtein kinase activityCyclin-dependent kinasesCell cycle progressionGenetic interactionsMitotic cyclinsTranscription factorsS. cerevisiaeKinase activityCycle progressionCell extractsG2 delayKinaseAltered expressionE. coliIntriguing possibilityPhosphorylationCyclinFull activityCak1pClb2TFIIHCak1
1993
Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro.
Connell-Crowley L, Solomon M, Wei N, Harper J. Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro. Molecular Biology Of The Cell 1993, 4: 79-92. PMID: 8443411, PMCID: PMC300902, DOI: 10.1091/mbc.4.1.79.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCDC2-CDC28 KinasesCyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclinsDNAEnzyme ActivationHumansIn Vitro TechniquesMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeXenopusXenopus ProteinsConceptsCDK2/cyclinCyclin-dependent kinase 2Cyclin AKinase 2Cyclin BPhosphorylation-independent activationSerine-threonine proteinCdc2/cyclin BCDK2/cyclin AHuman cyclin-dependent kinase 2G1/S transitionHistone H1 kinaseCyclin B complexCell cycle progressionSpecific activityCyclin bindingRecombinant CDK2Mammalian cellsH1 kinaseBacterial expressionT160 phosphorylationCycle progressionXenopus eggsCell extractsCyclin