2023
Identification of Protein Tyrosine Phosphatase (PTP) Substrates
Perla S, Qiu B, Dorry S, Yi J, Bennett A. Identification of Protein Tyrosine Phosphatase (PTP) Substrates. Methods In Molecular Biology 2023, 2743: 123-133. PMID: 38147212, DOI: 10.1007/978-1-0716-3569-8_8.Peer-Reviewed Original ResearchTeaching an old dog new tricks: A new tool for protein tyrosine phosphatase substrate discovery
Bennett A. Teaching an old dog new tricks: A new tool for protein tyrosine phosphatase substrate discovery. Journal Of Biological Chemistry 2023, 299: 104731. PMID: 37080392, PMCID: PMC10193000, DOI: 10.1016/j.jbc.2023.104731.Peer-Reviewed Original ResearchMeSH KeywordsMutationPhosphorylationProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesProteinsSignal TransductionSubstrate SpecificityConceptsIdentification of substratesSubstrate discoveryProtein tyrosineProtein substratesInteraction networksBreast cancer cell modelsCancer cell modelsFunctional interactionNovel targetVersatile new toolNew toolCell modelComplete understandingRecent studiesOld dog new tricksNew tricksInteractorsPTP1B.PTP1BPTPMutationsSubstrateEnzymeTyrosinePathwayMitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable?
Shillingford S, Bennett A. Mitogen-Activated Protein Kinase Phosphatases: No Longer Undruggable? The Annual Review Of Pharmacology And Toxicology 2023, 63: 617-636. PMID: 36662585, PMCID: PMC10127142, DOI: 10.1146/annurev-pharmtox-051921-121923.Peer-Reviewed Original ResearchMeSH KeywordsHumansMitogen-Activated Protein Kinase PhosphatasesNeoplasmsProtein Tyrosine PhosphatasesSignal TransductionConceptsMitogen-activated protein kinaseSmall molecule inhibitionProtein kinaseCritical cellular functionsInhibition of PTPsProtein tyrosineCellular functionsProtein substratesPhosphorylated proteinsCell signalingTyrosine residuesAttractive therapeutic targetCellular effectsKinaseNumerous diseasesPTPDiscovery toolTherapeutic developmentTherapeutic targetMetabolic diseasesInhibitionDephosphorylationSignalingMKPProtein
2022
A novel site on dual-specificity phosphatase MKP7/DUSP16 is required for catalysis and MAPK binding
Shillingford S, Zhang L, Surovtseva Y, Dorry S, Lolis E, Bennett AM. A novel site on dual-specificity phosphatase MKP7/DUSP16 is required for catalysis and MAPK binding. Journal Of Biological Chemistry 2022, 298: 102617. PMID: 36272649, PMCID: PMC9676401, DOI: 10.1016/j.jbc.2022.102617.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseP38 mitogen-activated protein kinaseMAPK bindingRegulatory mechanismsAllosteric siteMKP family membersNovel allosteric siteSmall molecule targetingMAPK/JNKAdditional regulatory mechanismsPhosphatase functionPhosphatase domainP38 MAPK/JNKProtein kinaseMKP7Site mutantsMAPK signalingAllosteric pocketMolecule targetingMAPK dephosphorylationMutantsNovel siteJNKCatalytic siteDephosphorylation
2014
Mining the function of protein tyrosine phosphatases in health and disease
Lee H, Yi JS, Lawan A, Min K, Bennett AM. Mining the function of protein tyrosine phosphatases in health and disease. Seminars In Cell And Developmental Biology 2014, 37: 66-72. PMID: 25263013, PMCID: PMC4339398, DOI: 10.1016/j.semcdb.2014.09.021.Peer-Reviewed Original ResearchConceptsPTP functionProtein tyrosineHuman diseasesProteomic approachNon-biased approachUnanticipated roleProteomic techniquesProteomic technologiesNovel therapeutic targetPTPTherapeutic targetTyrosineFundamental cellCrucial roleHuman healthDiscoveryRegulationRoleElucidationFunctionCellsCutting-edge technologiesTarget
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
1997
Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases
Bennett A, Tonks N. Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases. Science 1997, 278: 1288-1291. PMID: 9360925, DOI: 10.1126/science.278.5341.1288.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell Cycle ProteinsCell DifferentiationCell DivisionCell LineCloning, MolecularCulture MediaCyclin D1Dual Specificity Phosphatase 1Gene Expression Regulation, DevelopmentalImmediate-Early ProteinsJNK Mitogen-Activated Protein KinasesMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesMitogensMuscle ProteinsMuscle, SkeletalPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Tyrosine PhosphatasesRecombinant Fusion ProteinsSignal TransductionTetracyclineTranscription, GeneticConceptsMuscle-specific gene expressionMAPK phosphatase-1Skeletal muscle differentiationMuscle differentiationGene expressionMitogen-Activated Protein KinaseMuscle-specific genesSignal transduction pathwaysMKP-1 overexpressionPhosphatase 1Extracellular signalsProtein kinaseTransduction pathwaysMitogen withdrawalC2C12 myoblastsDifferentiated myocytesMyotube formationEndogenous expressionMyosin heavy chainMyogenesisDifferentiationHeavy chainExpressionOverexpressionAppropriate expression
1996
Multiple Requirements for SHPTP2 in Epidermal Growth Factor-Mediated Cell Cycle Progression
Bennett A, Hausdorff S, O’Reilly A, Freeman R, Neel B. Multiple Requirements for SHPTP2 in Epidermal Growth Factor-Mediated Cell Cycle Progression. Molecular And Cellular Biology 1996, 16: 1189-1202. PMID: 8622663, PMCID: PMC231101, DOI: 10.1128/mcb.16.3.1189.Peer-Reviewed Original ResearchConceptsElk-1 transactivationS-phase entryMitogen-activated proteinMAP kinase activationGrowth factorKinase activationFusion proteinPlatelet-derived growth factorGlutathione S-transferase fusion proteinEpidermal growth factor stimulationS-transferase fusion proteinProtein tyrosine phosphatase activityTyrosyl phosphorylation sitesGrowth factor stimulationSignal transduction pathwaysSerum-induced S-phase entryGrowth factor signalingImmediate early responseNIH 3T3 cellsCell cycle progressionEpidermal growth factorSH2 domainPhosphorylation sitesEGF stimulationTransduction pathways
1995
Different Signaling Roles of SHPTP2 in Insulin-induced GLUT1 Expression and GLUT4 Translocation ∗
Hausdorff S, Bennett A, Neel B, Birnbaum M. Different Signaling Roles of SHPTP2 in Insulin-induced GLUT1 Expression and GLUT4 Translocation ∗. Journal Of Biological Chemistry 1995, 270: 12965-12968. PMID: 7768884, DOI: 10.1074/jbc.270.22.12965.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsBase SequenceBiological TransportDNA PrimersGlucose Transporter Type 1Glucose Transporter Type 4InsulinIntracellular Signaling Peptides and ProteinsMiceMicroinjectionsMolecular Sequence DataMonosaccharide Transport ProteinsMuscle ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesRNA, MessengerSignal TransductionConceptsGLUT4 translocationNon-transmembrane protein tyrosine phosphataseSrc homology 2 domainGlutathione S-transferase fusion proteinS-transferase fusion proteinC-terminal SH2 domainCell surface GLUT1Insulin receptor substrate-1Cell surfaceProtein tyrosine phosphataseInsulin-stimulated mitogenesisTranslocation of GLUT4Insulin-stimulated expressionReceptor substrate-1Insulin-induced DNA synthesisInsulin-stimulated increaseNIH 3T3 fibroblastsSH2 domainSHPTP2Signaling roleSubstrate-1Fusion proteinInsulin stimulationMetabolic pathwaysIndependent pathways
1994
Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.
Bennett A, Tang T, Sugimoto S, Walsh C, Neel B. Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 7335-7339. PMID: 8041791, PMCID: PMC44394, DOI: 10.1073/pnas.91.15.7335.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsBase SequenceBinding SitesCell LineDNAGenes, rasHumansIntracellular Signaling Peptides and ProteinsMiceMice, Inbred BALB CMolecular Sequence DataPhosphorylationProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesReceptors, Platelet-Derived Growth FactorSH2 Domain-Containing Protein Tyrosine PhosphatasesSignal TransductionConceptsPlatelet-derived growth factor receptor betaGrowth factor receptor betaPDGF stimulationPositive signalingReceptor tyrosine kinasesSH2 domainRas activationGrowth factor receptorReceptor betaTyrosine phosphorylationSHPTP2Gene productsTyrosine kinaseGrb2Vivo sitesFactor receptorPhosphorylationSignalingPositive signalsSOS1RAHomologuesKinaseSite displayBeta
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 ResearchMeSH KeywordsAnimalsBinding SitesCells, CulturedDogsEnzyme ActivationHumansPhosphotyrosineProtein Tyrosine PhosphatasesReceptors, Platelet-Derived Growth FactorTyrosineConceptsSH-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