2007
Identification of Yeast IQGAP (Iqg1p) as an Anaphase-Promoting-Complex Substrate and Its Role in Actomyosin-Ring-Independent Cytokinesis
Ko N, Nishihama R, Tully GH, Ostapenko D, Solomon MJ, Morgan DO, Pringle JR. Identification of Yeast IQGAP (Iqg1p) as an Anaphase-Promoting-Complex Substrate and Its Role in Actomyosin-Ring-Independent Cytokinesis. Molecular Biology Of The Cell 2007, 18: 5139-5153. PMID: 17942599, PMCID: PMC2096582, DOI: 10.1091/mbc.e07-05-0509.Peer-Reviewed Original ResearchMeSH KeywordsActomyosinAmino Acid MotifsAnaphase-Promoting Complex-CyclosomeCytokinesisGene Expression Regulation, FungalMicrotubule-Associated ProteinsMutationMyosin Heavy ChainsPhenotypeProtein BindingRas GTPase-Activating ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityUbiquitinUbiquitin-Protein Ligase ComplexesConceptsActomyosin ringAPC/C mutantsAPC/C functionSeptin-dependent mannerAnaphase-promoting complexYeast Saccharomyces cerevisiaeOnset of cytokinesisDeletion of genesBud neckMitotic exitAPC/Mitotic cyclinsSaccharomyces cerevisiaeSeptum formationIqg1pCytokinesisNovel recognition sequenceC mutantsNonessential componentsSame phenotypeRecognition sequenceLate G1Rich mediumStrain backgroundComplex substratesMethods in cell cycle research
Solomon M, Cohen-Fix O. Methods in cell cycle research. Methods 2007, 41: 141-142. PMID: 17189855, DOI: 10.1016/j.ymeth.2006.07.021.Peer-Reviewed Original Research
2002
The anaphase-promoting complex: it's not just for mitosis any more
Harper J, Burton J, Solomon M. The anaphase-promoting complex: it's not just for mitosis any more. Genes & Development 2002, 16: 2179-2206. PMID: 12208841, DOI: 10.1101/gad.1013102.Peer-Reviewed Original ResearchAnaphase-Promoting Complex-CyclosomeAnimalsCdc20 ProteinsCdh1 ProteinsCell CycleCell Cycle ProteinsCyclin-Dependent KinasesHumansLigasesMitosisModels, BiologicalModels, MolecularPeptide SynthasesPhosphorylationProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSKP Cullin F-Box Protein LigasesUbiquitinUbiquitin-Protein Ligase Complexes
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 cellsThe role of Thr160 phosphorylation of Cdk2 in substrate recognition
Holmes J, Solomon M. The role of Thr160 phosphorylation of Cdk2 in substrate recognition. The FEBS Journal 2001, 268: 4647-4653. PMID: 11532001, DOI: 10.1046/j.1432-1327.2001.02392.x.Peer-Reviewed Original Research
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 200KinasePhosphorylationCDK6Kinetic 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 ResearchThe 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 defectCAKKinaseSerineThreonineHsl1p, 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 degradationKinaseCdc20pAnalysis 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
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 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 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
1997
Reduction of Background in Protein Kinase Assays by Electroblotting
Enke D, Solomon M. Reduction of Background in Protein Kinase Assays by Electroblotting. BioTechniques 1997, 22: 74-78. PMID: 8994651, DOI: 10.2144/97221bm15.Peer-Reviewed Original Research
1996
A Predictive Scale for Evaluating Cyclin-dependent Kinase Substrates A COMPARISON OF p34 cdc2 AND p33 cdk2 *
Holmes J, Solomon M. A Predictive Scale for Evaluating Cyclin-dependent Kinase Substrates A COMPARISON OF p34 cdc2 AND p33 cdk2 *. Journal Of Biological Chemistry 1996, 271: 25240-25246. PMID: 8810285, DOI: 10.1074/jbc.271.41.25240.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCDC2 Protein KinaseCDC2-CDC28 KinasesCell CycleCell LineConsensus SequenceCyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclinsGlutathione TransferaseHumansMutagenesis, Site-DirectedOligopeptidesPolymerase Chain ReactionProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSpodopteraSubstrate SpecificityTransfectionXenopusXenopus ProteinsConceptsSubstrate specificityDistinct substrate specificitiesPrimary sequence determinantsCyclin-dependent kinasesCDK substratesCyclin subunitProtein phosphorylationProtein kinaseCDK familyP34 cdc2Consensus sequenceSequence determinantsCell cyclePhosphorylation efficiencyKinasePeptide fusionsPhosphorylation potentialSignificant oversimplificationCdc2PhosphorylationSpecificitySubunitsCDK2SpeciesTrue specificity