2001
SHP-2 complex formation with the SHP-2 substrate-1 during C2C12 myogenesis.
Kontaridis M, Liu X, Zhang L, Bennett A. SHP-2 complex formation with the SHP-2 substrate-1 during C2C12 myogenesis. Journal Of Cell Science 2001, 114: 2187-98. PMID: 11493654, DOI: 10.1242/jcs.114.11.2187.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsAntigens, DifferentiationCell DifferentiationCell LineFibroblastsInsulinIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMiceMitogen-Activated Protein KinasesMolecular WeightMuscle, SkeletalMyoD ProteinNeural Cell Adhesion Molecule L1Neural Cell Adhesion Moleculesp38 Mitogen-Activated Protein KinasesPhosphoproteinsPhosphorylationPhosphotyrosineProtein BindingProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesReceptors, ImmunologicSH2 Domain-Containing Protein Tyrosine PhosphatasesSignal TransductionSomatomedinsConceptsSHP-2Tyrosyl phosphorylationSH2 domain-containing tyrosine phosphataseC2C12 myoblastsSubstrate-1MyoD-responsive genesMitogen-activated protein kinase activityP38 mitogen-activated protein kinase activityMuscle-specific genesProtein tyrosine kinasesSkeletal muscle differentiationProtein kinase activityExpression of MyoD.Cell-cell recognitionComplex formationInvolvement of tyrosineTyrosine phosphataseGab-1C2C12 myogenesisMuscle differentiationBinder 1Kinase activityInducible activationMyoD expressionTyrosine kinase
1998
Epidermal Growth Factor Receptor and the Adaptor Protein p52Shc Are Specific Substrates of T-Cell Protein Tyrosine Phosphatase
Tiganis T, Bennett A, Ravichandran K, Tonks N. Epidermal Growth Factor Receptor and the Adaptor Protein p52Shc Are Specific Substrates of T-Cell Protein Tyrosine Phosphatase. Molecular And Cellular Biology 1998, 18: 1622-1634. PMID: 9488479, PMCID: PMC108877, DOI: 10.1128/mcb.18.3.1622.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein KinasesCell NucleusCOS CellsCytoplasmEndoplasmic ReticulumEpidermal Growth FactorErbB ReceptorsGRB2 Adaptor ProteinHeLa CellsHumansMiceMitogen-Activated Protein Kinase 1MutagenesisPhosphorylationPhosphotyrosineProtein Tyrosine Phosphatase, Non-Receptor Type 2Protein Tyrosine PhosphatasesProteinsProtein-Tyrosine KinasesShc Signaling Adaptor ProteinsSrc Homology 2 Domain-Containing, Transforming Protein 1Substrate SpecificityTyrosineConceptsT-cell protein tyrosine phosphataseSubstrate-trapping mutantEpidermal growth factor receptorProtein tyrosine phosphatasePTyr proteinsTyrosine phosphataseGrowth factor receptorPTP active siteTyrosine phosphorylated proteinsEGF-induced activationFactor receptorAlternative splicingCellular contextCOS cellsP52ShcNuclear formTC45Endoplasmic reticulumCatalytic acidSpecific substratesProteinMutantsComplex formationSpecific sitesEGF
1993
Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor.
Lechleider R, Sugimoto S, Bennett A, Kashishian A, Cooper J, Shoelson S, Walsh C, Neel B. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. Journal Of Biological Chemistry 1993, 268: 21478-21481. PMID: 7691811, DOI: 10.1016/s0021-9258(20)80562-6.Peer-Reviewed Original ResearchConceptsSH-PTP2Platelet-derived growth factor receptorGrowth factor receptorPhosphotyrosyl peptidesFactor receptorSrc homology 2 domainHuman platelet-derived growth factor receptorIntrinsic tyrosine kinase activityPeptide competition assaysTyrosine kinase activitySH2 domainPhosphorylation sitesSignal transductionKinase activityMajor binding siteImmunoprecipitation studiesCompetition assaysTyrosyl residuesBinding sitesEarly eventsProteinLigand additionActivity 5ReceptorsDocking point
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply