2001
CAK-independent Activation of CDK6 by a Viral Cyclin
Kaldis P, Ojala P, Tong L, Mäkelä T, Solomon M. CAK-independent Activation of CDK6 by a Viral Cyclin. Molecular Biology Of The Cell 2001, 12: 3987-3999. PMID: 11739795, PMCID: PMC60770, DOI: 10.1091/mbc.12.12.3987.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCyclin-Dependent Kinase 6Cyclin-Dependent Kinase Inhibitor p16Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsEnzyme ActivationFluorescent Antibody TechniqueHerpesvirus 8, HumanHumansPhosphorylationProtein ConformationProtein Serine-Threonine KinasesTumor Cells, CulturedViral ProteinsConceptsKSHV-cyclinSarcoma-associated herpesvirusKaposi's sarcoma-associated herpesvirusCell cycle progression independentAbsence of phosphorylationCyclin-dependent kinasesD-type cyclinsCAK phosphorylationExpression of CDK6CDK6 activationMitogenic signalsSubstrate specificityCell-based assaysCDK inhibitorsViral cyclinConformational changesCell deathPhosphorylationCAKCDK inhibitionKinaseCyclinCDK6Ternary complexNormal cells
2000
Kinetic Analysis of the Cyclin-dependent Kinase-activating Kinase (Cak1p) from Budding Yeast*
Enke D, Kaldis P, Solomon M. Kinetic Analysis of the Cyclin-dependent Kinase-activating Kinase (Cak1p) from Budding Yeast*. Journal Of Biological Chemistry 2000, 275: 33267-33271. PMID: 10934199, DOI: 10.1074/jbc.m004748200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateCatalysisCDC2-CDC28 KinasesCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesEnzyme StabilityKineticsPhosphorylationProtein Serine-Threonine KinasesSaccharomycetalesConceptsCyclin-dependent kinasesThe 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 ResearchMeSH KeywordsCDC2-CDC28 KinasesChromatography, AffinityCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesHeLa CellsHumansPhosphorylationProtein Serine-Threonine KinasesSubstrate SpecificityConceptsCdk-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
Transforming growth factor β targeted inactivation of cyclin E:cyclin-dependent kinase 2 (Cdk2) complexes by inhibition of Cdk2 activating kinase activity
Nagahara H, Ezhevsky S, Vocero-Akbani A, Kaldis P, Solomon M, Dowdy S. Transforming growth factor β targeted inactivation of cyclin E:cyclin-dependent kinase 2 (Cdk2) complexes by inhibition of Cdk2 activating kinase activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 14961-14966. PMID: 10611320, PMCID: PMC24755, DOI: 10.1073/pnas.96.26.14961.Peer-Reviewed Original ResearchMeSH KeywordsCDC2-CDC28 KinasesCyclin ECyclin HCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsDown-RegulationEnzyme ActivationG1 PhaseHumansModels, BiologicalPhosphorylationProtein Serine-Threonine KinasesThreonineTransforming Growth Factor betaTumor Cells, CulturedConceptsTGF-beta treatmentInhibition of CDK2Cyclin ECyclin DGrowth factor betaGrowth factor βHepG2 hepatocellular carcinoma cellsHepatocellular carcinoma cellsTGF-beta signalingHuman HepG2 hepatocellular carcinoma cellsFactor betaCarcinoma cellsCyclin-dependent kinase 2 complexFactor βKinase activityCDK7 activityCDK4/6 activityHepG2 cellsWhole cell lysatesTumor suppressor proteinCDK2TreatmentCdk2 complexesArrestCellsDephosphorylation 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 extractsKinasePP2CDephosphorylationPhosphorylationPhosphatasePTC2Ptc2pActivating Phosphorylation of the Kin28p Subunit of Yeast TFIIH by Cak1p
Kimmelman J, Kaldis P, Hengartner C, Laff G, Koh S, Young R, Solomon M. Activating Phosphorylation of the Kin28p Subunit of Yeast TFIIH by Cak1p. Molecular And Cellular Biology 1999, 19: 4774-4787. PMID: 10373527, PMCID: PMC84276, DOI: 10.1128/mcb.19.7.4774.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell CycleCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesEnzyme ActivationPhosphorylationPoint MutationProtein Serine-Threonine KinasesRabbitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsThreonineTranscription Factor TFIIDTranscription Factor TFIIHTranscription FactorsTranscription Factors, TFIIConceptsKinase activityGeneral transcription factor TFIIHTranscription factor TFIIHCTD kinase activityRNA polymerase IICell cycle CDKsCyclin-dependent kinasesPrevious biochemical observationsYeast TFIIHPolymerase IIActivating PhosphorylationLarge subunitCak1pCatalytic subunitKinase subunitTerminal domainTFIIHConditional alleleCell cyclePhosphorylationCAKSubunitsCDKMO15KinaseThe CDK-activating Kinase (Cak1p) from Budding Yeast Has an Unusual ATP-binding Pocket*
Enke D, Kaldis P, Holmes J, Solomon M. The CDK-activating Kinase (Cak1p) from Budding Yeast Has an Unusual ATP-binding Pocket*. Journal Of Biological Chemistry 1999, 274: 1949-1956. PMID: 9890950, DOI: 10.1074/jbc.274.4.1949.Peer-Reviewed Original ResearchConceptsProtein kinaseInvariant lysineMajor cyclin-dependent kinaseLoop regionEssential protein kinaseMost protein kinasesAmino acidsATP-binding pocketCyclin-dependent kinasesBudding YeastCak1pMutagenic analysisATP phosphatesSequence differencesLoop motifKinaseCovalent modificationCore sequenceATP analogYeastCatalytic rateInhibitory drugsLysineMutationsATP
1998
Localization and regulation of the cdk-activating kinase (Cak1p) from budding yeast
Kaldis P, Pitluk Z, Bany I, Enke D, Wagner M, Winter E, Solomon M. Localization and regulation of the cdk-activating kinase (Cak1p) from budding yeast. Journal Of Cell Science 1998, 111: 3585-3596. PMID: 9819350, DOI: 10.1242/jcs.111.24.3585.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCDC28 Protein Kinase, S cerevisiaeCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCytoplasmFluorescent Antibody TechniqueGene Expression Regulation, FungalIsoelectric FocusingMeiosisMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSubcellular FractionsConceptsBiochemical subcellular fractionationEukaryotic cell cyclePost-translational levelCyclin-dependent kinasesMajor CdkThreonine 169Two-dimensional isoelectric focusingCak1pPosttranslational modificationsStable proteinSubcellular fractionationMonomeric enzymeCell cycleYeastCDKKinaseCAKFurther characterizationPhosphorylationRegulationIsoelectric focusingPotential sitesCdc28pCellsMeiosisHuman 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 ResearchMeSH KeywordsCDC2-CDC28 KinasesCyclin-Dependent Kinase 2Cyclin-Dependent Kinase 6Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsEnzyme ActivationHumansPhosphorylationProtein Serine-Threonine KinasesSubstrate SpecificityYeastsConceptsTranscription 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 inhibitorsCDKCyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases
Egan E, Solomon M. Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases. Molecular And Cellular Biology 1998, 18: 3659-3667. PMID: 9632748, PMCID: PMC108948, DOI: 10.1128/mcb.18.7.3659.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCDC2 Protein KinaseCDC2-CDC28 KinasesCell Cycle ProteinsCyclin ACyclin BCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesEnzyme ActivationPhosphorylationProtein BindingProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsThreonineXenopusXenopus Proteins
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 SequenceCDC2-CDC28 KinasesCDC28 Protein Kinase, S cerevisiaeCell 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
1994
p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest.
Polyak K, Kato J, Solomon M, Sherr C, Massague J, Roberts J, Koff A. p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest. Genes & Development 1994, 8: 9-22. PMID: 8288131, DOI: 10.1101/gad.8.1.9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCDC2-CDC28 KinasesCell CommunicationCell CycleCell LineCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsMinkProtein Kinase InhibitorsProtein KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProteinsSignal TransductionTransforming Growth Factor betaConceptsCdk2 complexesCyclin ECyclin D2-Cdk4 complexesCyclin-Cdk inhibitorCell-cell contactGrowth inhibitory signalsCell cycle arrestCatalytic subunitG1 progressionG1 cyclinsCell cycleCdk2 activationCycle arrestCDK2 inhibitionContact inhibitionCyclin E levelsActive complexAffinity chromatographyEpithelial cellsCDK2Inhibitory signalsCellsP27ComplexesActivation
1993
CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15.
Solomon M, Harper J, Shuttleworth J. CAK, the p34cdc2 activating kinase, contains a protein identical or closely related to p40MO15. The EMBO Journal 1993, 12: 3133-3142. PMID: 8344252, PMCID: PMC413579, DOI: 10.1002/j.1460-2075.1993.tb05982.x.Peer-Reviewed Original Research