2007
Use of a Chemical Genetic Technique To Identify Myosin IIB as a Substrate of the Abl-Related Gene (Arg) Tyrosine Kinase
Boyle SN, Koleske AJ. Use of a Chemical Genetic Technique To Identify Myosin IIB as a Substrate of the Abl-Related Gene (Arg) Tyrosine Kinase. Biochemistry 2007, 46: 11614-11620. PMID: 17892306, DOI: 10.1021/bi701119s.Peer-Reviewed Original ResearchConceptsPutative substratesMyosin IIBGene Tyrosine KinaseUnnatural ATP analoguesProtein substrate specificityPhosphotyrosine-containing proteinsSer/ThrAbl/ArgChemical-genetic techniqueCell morphogenesisKinase substrateDirect substrateFamily kinasesTyrosine phosphorylationSubstrate specificityGenetic techniquesNucleotide specificityMolecular mechanismsTyrosine kinaseK-252aUnexpected high levelATP analogGene kinaseKinaseABL
2004
Bidirectional Signaling Links the Abelson Kinases to the Platelet-Derived Growth Factor Receptor
Plattner R, Koleske AJ, Kazlauskas A, Pendergast AM. Bidirectional Signaling Links the Abelson Kinases to the Platelet-Derived Growth Factor Receptor. Molecular And Cellular Biology 2004, 24: 2573-2583. PMID: 14993293, PMCID: PMC355852, DOI: 10.1128/mcb.24.6.2573-2583.2004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineChemotaxisEnzyme ActivationIn Vitro TechniquesMacromolecular SubstancesMiceNIH 3T3 CellsPhospholipase C gammaPhosphorylationProtein-Tyrosine KinasesProto-Oncogene Proteins c-ablReceptor, Platelet-Derived Growth Factor alphaReceptor, Platelet-Derived Growth Factor betaRecombinant ProteinsSignal TransductionType C PhospholipasesConceptsPDGF beta receptorPlatelet-derived growth factorC-AblPLC-gamma1C-Abl nonreceptor tyrosine kinaseTyrosine kinaseGrowth factor signalsSrc family kinasesC-Abl functionNonreceptor tyrosine kinaseTyrosine kinase activityPlatelet-derived growth factor receptorAbundant phosphoinositideMembrane rufflingInducible complexNonredundant functionsFamily kinasesMembrane proteinsC-gamma1Factor signalsGrowth factor receptorAbelson kinaseKinase activityBiological processesChemotaxis defect
2003
Phospholipids Can Switch the GTPase Substrate Preference of a GTPase-activating Protein*
Ligeti E, Dagher MC, Hernandez SE, Koleske AJ, Settleman J. Phospholipids Can Switch the GTPase Substrate Preference of a GTPase-activating Protein*. Journal Of Biological Chemistry 2003, 279: 5055-5058. PMID: 14699145, DOI: 10.1074/jbc.c300547200.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsSmall GTPasesSubstrate preferencePotent GTPase-activating proteinMajor cellular inhibitorActivity of GTPasesNovel regulatory mechanismLikely physiological roleRacGAP activityIntrinsic GTPRhoGAP activityP190 RhoGAPCellular inhibitorRac GTPasesGTPasesRegulatory mechanismsPhysiological roleProteinPhospholipidsFatty acidsRhoGAPGTPP190ActivityRho
1993
A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast
Thompson C, Koleske A, Chao D, Young R. A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast. Cell 1993, 73: 1361-1375. PMID: 8324825, DOI: 10.1016/0092-8674(93)90362-t.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesDNA Mutational AnalysisDNA-Binding ProteinsFungal ProteinsGene Expression RegulationMediator ComplexMolecular Sequence DataMultienzyme ComplexesRecombinant ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription FactorsTranscription, GeneticConceptsTATA-binding proteinRNA polymerase II carboxy-terminal domainCarboxy-terminal domainMultisubunit complexLarge multisubunit complexFunctional preinitiation complexRNA polymerase IIEfficient transcription initiationTranscription initiation complexSRB proteinsCTD proteinsExtragenic suppressorsCTD functionPolymerase IIPreinitiation complexTranscription initiationInitiation complexComplex bindsTruncation mutationsSRB2Srb5ProteinBiochemical evidenceComplexesSRB4