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 200KinasePhosphorylationCDK6The 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
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 extractsKinasePP2CDephosphorylationPhosphorylationPhosphatasePTC2Ptc2p