2000
Dephosphorylation of Human Cyclin-dependent Kinases by Protein Phosphatase Type 2Cα and β2 Isoforms*
Cheng A, Kaldis P, Solomon M. Dephosphorylation of Human Cyclin-dependent Kinases by Protein Phosphatase Type 2Cα and β2 Isoforms*. Journal Of Biological Chemistry 2000, 275: 34744-34749. PMID: 10934208, DOI: 10.1074/jbc.m006210200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsChromatography, Ion ExchangeCyclin-Dependent KinasesCyclinsHeLa CellsHumansIsoenzymesMiceMolecular Sequence DataPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2Protein Phosphatase 2CRatsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSubstrate SpecificityConceptsHeLa cell extractsCyclin-dependent kinasesPP2C alphaType 2C protein phosphatasesHuman cyclin-dependent kinaseCell extractsBeta 2 isoformBinding of cyclinsDephosphorylation of cdk2Mono Q chromatographyBeta 2 proteinProtein phosphataseThreonine residuesSubstrate preferenceBeta 2Beta isoformsΒ2 isoformPhosphatase activityIsoformsDephosphorylationDEAE-SepharoseSuperdex 200KinasePhosphorylationCDK6Hsl1p, a Swe1p Inhibitor, Is Degraded via the Anaphase-Promoting Complex
Burton J, Solomon M. Hsl1p, a Swe1p Inhibitor, Is Degraded via the Anaphase-Promoting Complex. Molecular And Cellular Biology 2000, 20: 4614-4625. PMID: 10848588, PMCID: PMC85864, DOI: 10.1128/mcb.20.13.4614-4625.2000.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAnaphase-Promoting Complex-CyclosomeApc8 Subunit, Anaphase-Promoting Complex-CyclosomeBase SequenceCdc20 ProteinsCdh1 ProteinsCell CycleCell Cycle ProteinsCyclin-Dependent KinasesFungal ProteinsGenes, DominantLigasesMolecular Sequence DataMutationPrecipitin TestsProtein KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesYeastsConceptsAnaphase-promoting complexDestruction box motifCell cycle eventsProtein kinaseBox motifCycle eventsCyclin-dependent kinase Cdc28pCritical cell cycle regulatorsAPC-dependent mannerCell cycle regulatorsSwe1p degradationMorphogenesis checkpointAPC substratesHsl1pLate mitosisProper progressionProtein substratesUbiquitin ligaseCoimmunoprecipitation studiesSequence homologyCycle regulatorsUbiquitinationSubsequent degradationKinaseCdc20p
1999
The 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 sitesCdc28pCellsMeiosis
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
1995
KIN28 Encodes a C-Terminal Domain Kinase That Controls mRNA Transcription in Saccharomyces cerevisiae but Lacks Cyclin-Dependent Kinase-Activating Kinase (CAK) Activity
Cismowski M, Laff G, Solomon M, Reed S. KIN28 Encodes a C-Terminal Domain Kinase That Controls mRNA Transcription in Saccharomyces cerevisiae but Lacks Cyclin-Dependent Kinase-Activating Kinase (CAK) Activity. Molecular And Cellular Biology 1995, 15: 2983-2992. PMID: 7760796, PMCID: PMC230529, DOI: 10.1128/mcb.15.6.2983.Peer-Reviewed Original ResearchConceptsC-terminal domainKinase activityCTD kinaseMRNA transcriptionCritical threonine residueCyclin-dependent kinase familyCTD kinase activityRNA polymerase IICell cycle CDKsExtensive sequence identityCyclin-dependent kinasesThermosensitive alleleCTD phosphorylationPolymerase IIThreonine residuesKinase familyPositive regulatorKin28Phosphorylation stateS. cerevisiaeSequence identityCell cycleTranscriptionHuman cellsCDK
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 ResearchPhosphorylation 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