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
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 defectCAKKinaseSerineThreonine
1999
Activating 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 cyclePhosphorylationCAKSubunitsCDKMO15Kinase
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 sitesCdc28pCellsMeiosis
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