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 substrates
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
2000
Activating 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 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 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
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
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