2000
Hsl1p, 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 degradationKinaseCdc20pActivating 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 extractsKinasePP2CDephosphorylationPhosphorylationPhosphatasePTC2Ptc2pThe 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
Cyclin-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
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
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