1993
Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro.
Macdonald SG, Crews CM, Wu L, Driller J, Clark R, Erikson RL, McCormick F. Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro. Molecular And Cellular Biology 1993, 13: 6615-6620. PMID: 8413257, PMCID: PMC364724, DOI: 10.1128/mcb.13.11.6615.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBaculoviridaeCell LineCloning, MolecularGenes, rasGenes, srcHumansMAP Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesMothsMutagenesis, Site-DirectedPhosphorylationPolymerase Chain ReactionProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-rafProto-Oncogene Proteins p21(ras)Recombinant ProteinsSignal TransductionTransfectionConceptsRaf-1V-SrcV-rasSf9 cellsGlutathione S-transferase fusion proteinS-transferase fusion proteinSerine/threonine kinaseProtein kinase C phosphorylationKinase-inactive versionERK signal transduction pathwayKinase-inactive mutantRaf-1 phosphorylationKinase C phosphorylationSignal transduction pathwaysRaf-1-MEKActivation of MEKTyrosine kinase oncogenesProtein kinase CAutokinase activityFunction upstreamThreonine kinaseDirect substrateMEK activationTransduction pathwaysC phosphorylationReconstitution of the Raf-1-MEK-ERK Signal Transduction Pathway In Vitro
MacDonald S, Crews C, Wu L, Driller J, Clark R, Erikson R, McCormick F. Reconstitution of the Raf-1-MEK-ERK Signal Transduction Pathway In Vitro. Molecular And Cellular Biology 1993, 13: 6615-6620. DOI: 10.1128/mcb.13.11.6615-6620.1993.Peer-Reviewed Original ResearchRaf-1V-SrcV-rasSf9 cellsGlutathione S-transferase fusion proteinS-transferase fusion proteinSerine/threonine kinaseProtein kinase C phosphorylationKinase-inactive versionERK signal transduction pathwayKinase-inactive mutantRaf-1 phosphorylationKinase C phosphorylationSignal transduction pathwaysRaf-1-MEKActivation of MEKTyrosine kinase oncogenesProtein kinase CAutokinase activityFunction upstreamThreonine kinaseDirect substrateMEK activationTransduction pathwaysC phosphorylation
1992
Phorbol ester stimulates a protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product.
Alessandrini A, Crews CM, Erikson RL. Phorbol ester stimulates a protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 8200-8204. PMID: 1518847, PMCID: PMC49885, DOI: 10.1073/pnas.89.17.8200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCells, CulturedIn Vitro TechniquesMiceMitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesPeptide MappingPhorbol EstersPhosphorylationPhosphothreonineProtein KinasesProtein-Tyrosine KinasesT-LymphocytesConceptsProtein kinase activityProtein kinaseGene productsKinase activityMyelin basic protein kinaseMyelin basic protein kinase activityMultiple extracellular signalsUpstream protein kinaseWild-type proteinIdentification of proteinsAmino acid residuesSame amino acid residuesERK-1 proteinDegree of phosphorylationReversible phosphorylationThreonine sitesThreonine kinaseExtracellular signalsTyrosine sitesAcid residuesKinasePhosphorylationPhorbol esterProteinThreoninePurification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product.
Crews CM, Erikson RL. Purification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 8205-8209. PMID: 1381507, PMCID: PMC49886, DOI: 10.1073/pnas.89.17.8205.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsEnzyme ActivationFungal ProteinsGenesMiceMitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesMolecular Sequence DataPeptide FragmentsPhosphorylationPhosphoserinePhosphothreoninePhosphotyrosineProtein KinasesRecombinant ProteinsSequence AlignmentTyrosineConceptsGene productsProtein kinaseSerine/threonine phosphatase 2AMyelin basic protein kinaseProtein tyrosine phosphatase 1B.MAPK/ERK kinaseSignal transduction mechanismsPossible signal transduction mechanismsERK-1 proteinSte7 genePhosphatase 2AThreonine kinaseERK kinaseERK-1Tyrosine residuesSequence analysisKinaseTransduction mechanismsMEKTrypsin digestionProteinByr1PurificationGenesLesser extent
1991
Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine.
Crews CM, Alessandrini AA, Erikson RL. Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 8845-8849. PMID: 1717989, PMCID: PMC52607, DOI: 10.1073/pnas.88.19.8845.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBlotting, WesternCalcium-Calmodulin-Dependent Protein KinasesCloning, MolecularMiceMolecular Sequence DataMolecular WeightMyelin Basic ProteinOligonucleotidesPhosphoprotein PhosphatasesPhosphoproteinsPhosphotyrosinePolymerase Chain ReactionProtein KinasesProtein Phosphatase 2Protein Serine-Threonine KinasesRecombinant ProteinsTyrosineConceptsSerine/threonine protein kinaseERK-1Serine/threonine kinaseRibosomal protein S6 kinaseSubstrate phosphorylation sitesThreonine protein kinaseProtein S6 kinaseSame substrate specificityPhosphatase 2AThreonine residuesThreonine kinaseActive kinasePhosphorylation sitesERK1 proteinS6 kinaseProtein kinaseSequence dataBacterial expressionSubstrate specificityGene productsKinase activityPhosphatase 1BKinaseRat cellsProtein