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
2001
The 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 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 defectCAKKinaseSerineThreonineAnalysis 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 analogKinaseSubunits
1998
Human 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 inhibitorsCDK
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