2007
Status Epilepticus-Induced Somatostatinergic Hilar Interneuron Degeneration Is Regulated by Striatal Enriched Protein Tyrosine Phosphatase
Choi YS, Lin SL, Lee B, Kurup P, Cho HY, Naegele JR, Lombroso PJ, Obrietan K. Status Epilepticus-Induced Somatostatinergic Hilar Interneuron Degeneration Is Regulated by Striatal Enriched Protein Tyrosine Phosphatase. Journal Of Neuroscience 2007, 27: 2999-3009. PMID: 17360923, PMCID: PMC2701360, DOI: 10.1523/jneurosci.4913-06.2007.Peer-Reviewed Original ResearchConceptsStriatal-enriched protein tyrosine phosphataseERK/MAPK activationProtein tyrosine phosphataseCell deathTyrosine phosphataseExtracellular signal-regulated kinase/mitogen-activated protein kinase pathwayKinase/mitogen-activated protein kinase pathwayMAPK activationMAPK pathwayERK/MAPK signalingMitogen-activated protein kinase pathwayStriatal enriched protein tyrosine phosphataseProtein kinase pathwayNeuroprotective responseKinase pathwayImmediate early gene expressionKey regulatorMAPK signalingGene expressionMolecular mechanismsVivo disruptionSignificant rescuePathwayPhosphataseActivation
2006
The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala
Paul S, Olausson P, Venkitaramani DV, Ruchkina I, Moran TD, Tronson N, Mills E, Hakim S, Salter MW, Taylor JR, Lombroso PJ. The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala. Biological Psychiatry 2006, 61: 1049-1061. PMID: 17081505, PMCID: PMC1853327, DOI: 10.1016/j.biopsych.2006.08.005.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAminoacetonitrileAmygdalaAnimalsBehavior, AnimalCells, CulturedConditioning, ClassicalCycloheximideElectric StimulationEnzyme InhibitorsFearFemaleImmunohistochemistryIn Vitro TechniquesLong-Term PotentiationMemoryMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NeostriatumPatch-Clamp TechniquesPoint MutationPregnancyProtein Synthesis InhibitorsProtein Tyrosine PhosphatasesRatsRats, Sprague-DawleyTranslocation, GeneticConceptsStriatal-enriched protein tyrosine phosphataseERK1/2 activationMitogen-activated protein kinaseProtein tyrosine phosphataseDe novo translationActivation of ERK1/2Tyrosine phosphataseProtein bindsKinase signalingProtein kinaseSequential recruitmentAmygdala-dependent memory formationERK pathwayMemory formationPrimary cell culturesNuclear translocationBiphasic activationLong-term potentiationTranslation blockTAT-STEPERKCell culturesERK1/2ActivationPathwaySynaptic plasticity: one STEP at a time
Braithwaite SP, Paul S, Nairn AC, Lombroso PJ. Synaptic plasticity: one STEP at a time. Trends In Neurosciences 2006, 29: 452-458. PMID: 16806510, PMCID: PMC1630769, DOI: 10.1016/j.tins.2006.06.007.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsHumansModels, BiologicalNeuronal PlasticityProtein Tyrosine PhosphatasesSignal TransductionSynapses
2005
Regulation of NMDA receptor trafficking by amyloid-β
Snyder EM, Nong Y, Almeida CG, Paul S, Moran T, Choi EY, Nairn AC, Salter MW, Lombroso PJ, Gouras GK, Greengard P. Regulation of NMDA receptor trafficking by amyloid-β. Nature Neuroscience 2005, 8: 1051-1058. PMID: 16025111, DOI: 10.1038/nn1503.Peer-Reviewed Original ResearchMeSH KeywordsAlpha7 Nicotinic Acetylcholine ReceptorAlzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsCalcineurinCell MembraneCerebral CortexCREB-Binding ProteinDisease Models, AnimalElectric ConductivityEndocytosisEnzyme ActivationMiceNeuronsN-MethylaspartateNuclear ProteinsPeptide FragmentsProtein TransportProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorReceptors, NicotinicReceptors, N-Methyl-D-AspartateSignal TransductionSynapsesTrans-ActivatorsConceptsNMDA receptorsCortical neuronsAlzheimer's diseaseBrains of patientsAlzheimer's disease pathologyNMDA receptor traffickingGenetic mouse modelsΓ-secretase inhibitorApplication of amyloidSurface NMDA receptorsGlutamatergic transmissionSynaptic dysfunctionPersistent depressionTyrosine phosphatase STEPNicotinic receptorsMouse modelDisease processSynaptic plasticityDisease pathologyNeuronsReceptorsAmyloidSurface expressionUnderlying mechanismReceptor trafficking
2003
Receptor and nonreceptor protein tyrosine phosphatases in the nervous system
Paul S, Lombroso P. Receptor and nonreceptor protein tyrosine phosphatases in the nervous system. Cellular And Molecular Life Sciences 2003, 60: 2465-2482. PMID: 14625689, PMCID: PMC11138652, DOI: 10.1007/s00018-003-3123-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainHumansIntracellular Signaling Peptides and ProteinsMitogen-Activated Protein KinasesNerve Tissue ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorReceptor-Like Protein Tyrosine Phosphatases, Class 2Receptor-Like Protein Tyrosine Phosphatases, Class 5Receptors, Cell SurfaceSignal TransductionConceptsProtein tyrosineNonreceptor protein tyrosineDual-specific phosphataseCellular signaling pathwaysNervous systemSignaling pathwaysCellular localizationPhysiological functionsFunctional rolePTPCentral nervous systemIntracellular mechanismsTyrosineImportant rolePhosphatasePathwayRoleLocalizationFunctionReceptors
2000
The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway
Paul S, Snyder G, Yokakura H, Picciotto M, Nairn A, Lombroso P. The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway. Journal Of Neuroscience 2000, 20: 5630-5638. PMID: 10908600, PMCID: PMC6772528, DOI: 10.1523/jneurosci.20-15-05630.2000.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCatalytic DomainCorpus StriatumCyclic AMP-Dependent Protein KinasesEnzyme ActivationIn Vitro TechniquesMaleMolecular Sequence DataNeuronsPhosphoproteinsPhosphorus RadioisotopesPhosphorylationProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, Dopamine D1Signal TransductionConceptsProtein tyrosine phosphatase familyCAMP-dependent protein kinaseTryptic phosphopeptide mappingPotential phosphorylation sitesUnique N-terminalProtein-protein interactionsMembrane-associated proteinsRole of phosphorylationTyrosine phosphatase familyAmino acid sequenceSite-directed mutagenesisAmino acid sequencingPKA-dependent pathwayTyrosine phosphatase STEPPhosphatase familyPhosphopeptide mappingPhosphorylation sitesAlternative splicingSubcellular compartmentsProtein kinaseTerminal domainEquivalent residuesCytosolic proteinsSpecific residuesAcid sequence
1999
Hypoxia‐Ischemia in Perinatal Rat Brain Induces the Formation of a Low Molecular Weight Isoform of Striatal Enriched Tyrosine Phosphatase (STEP)
Gurd J, Bissoon N, Nguyen T, Lombroso P, Rider C, Beesley P, Vannucci S. Hypoxia‐Ischemia in Perinatal Rat Brain Induces the Formation of a Low Molecular Weight Isoform of Striatal Enriched Tyrosine Phosphatase (STEP). Journal Of Neurochemistry 1999, 73: 1990-1994. PMID: 10537057, DOI: 10.1046/j.1471-4159.1999.01990.x.Peer-Reviewed Original ResearchMeSH KeywordsAgingAnimalsFemaleHypoxia-Ischemia, BrainIsoenzymesMolecular WeightProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, WistarConceptsHypoxia-ischemiaP21 ratsRat brainIschemia-induced elevationP21 rat brainUnilateral hypoxia-ischemiaCerebral hypoxia-ischemiaPerinatal rat brainResult of ischemiaCalcium-dependent proteolysisLow molecular weight isoformsInterval of recoveryP7 ratsContralateral sideMolecular weight isoformsNT2/D1 cellsCalcium ionophoreLow Mr isoformPostsynaptic densityRatsBrainCalpain IWeight isoformsIschemiaPhosphorylation levelsCalcium‐Dependent Cleavage of Striatal Enriched Tyrosine Phosphatase (STEP)
Nguyen T, Paul S, Xu Y, Gurd J, Lombroso P. Calcium‐Dependent Cleavage of Striatal Enriched Tyrosine Phosphatase (STEP). Journal Of Neurochemistry 1999, 73: 1995-2001. PMID: 10537058, DOI: 10.1046/j.1471-4159.1999.01995.x.Peer-Reviewed Original ResearchConceptsPostsynaptic densityTransient hypoxia-ischemiaPrimary neuronal culturesNeuronal precursor cellsCalcium-dependent cleavageHypoxia-ischemiaStriatal neuronsNeuronal insultsRat striatumNeuronal culturesCalcium ionophoreCalpain inhibitorsSTEP61Precursor cellsLow molecular weight formMolecular weight formsPhosphorylation levelsSmaller isoformSignificant increaseTyrosine phosphorylation levelsRapid appearanceCalpain treatmentRapid influxWeight formsCells
1997
STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms.
Bult A, Zhao F, Dirkx R, Raghunathan A, Solimena M, Lombroso P. STEP: a family of brain-enriched PTPs. Alternative splicing produces transmembrane, cytosolic and truncated isoforms. European Journal Of Cell Biology 1997, 72: 337-44. PMID: 9127733.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernBlotting, WesternBrainCalcium-Binding ProteinsCalnexinCHO CellsCricetinaeFemaleFluorescent Antibody Technique, IndirectMembrane ProteinsMolecular Sequence DataProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsSynaptophysinTransfectionConceptsProtein tyrosine phosphataseCatalytic phosphatase domainProtein tyrosine kinase familyHydrophobic amino acid sequenceAlternative splicing mechanismAmino acid sequencePrevious biochemical studiesTyrosine kinase familyStop codon upstreamPhosphatase domainCytosolic variantAlternative splicingMembrane compartmentsTyrosine phosphataseKinase familySplicing mechanismSubcellular localizationCytosolic proteinsAcid sequenceN-terminusInactive variantContinuous sucrose gradientSTEP isoformsPolyproline domainEndoplasmic reticulum
1996
STEP61: A Member of a Family of Brain-Enriched PTPs Is Localized to the Endoplasmic Reticulum
Bult A, Zhao F, Dirkx R, Sharma E, Lukacsi E, Solimena M, Naegele J, Lombroso P. STEP61: A Member of a Family of Brain-Enriched PTPs Is Localized to the Endoplasmic Reticulum. Journal Of Neuroscience 1996, 16: 7821-7831. PMID: 8987810, PMCID: PMC6579237, DOI: 10.1523/jneurosci.16-24-07821.1996.Peer-Reviewed Original ResearchConceptsNovel N-terminal regionEnzymatic activityEndoplasmic reticulumPutative transmembrane domainsIntrinsic membrane proteinsExtended N-terminusAmino acid sequenceN-terminal regionDistinctive intracellular distributionsProtein tyrosineCytosolic variantTransmembrane domainMembrane compartmentsMembrane proteinsAcid sequenceSubcellular fractionationN-terminusRecombinant proteinsTransfection experimentsSTEP61Intracellular distributionProteinReticulumImmunocytochemical labelingFamilyTransient compartmental expression of a family of protein tyrosine phosphatases in the developing striatum
Raghunathan A, Matthews G, Lombroso P, Naegele J. Transient compartmental expression of a family of protein tyrosine phosphatases in the developing striatum. Brain Research 1996, 91: 190-199. PMID: 8852369, DOI: 10.1016/0165-3806(95)00176-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, NorthernBlotting, WesternCalbindinsCell CountDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsFemaleGene Expression Regulation, DevelopmentalIsoenzymesNeostriatumNerve Tissue ProteinsNeuronsPhosphoproteinsPostpartum PeriodPregnancyProtein Tyrosine PhosphatasesRatsRats, Inbred StrainsS100 Calcium Binding Protein GSubstance PSubstantia NigraTime FactorsTranscription, GeneticConceptsPatch neuronsPostnatal weekTwo-color immunofluorescent stainingTyrosine hydroxylase-immunoreactive fibersDopaminoceptive brain regionsCalbindin-positive neuronsHydroxylase-immunoreactive fibersStriatum of ratsDopamine islandsPostnatal day 1Most striatal neuronsFirst postnatal weekEarly postnatal developmentMatrix neuronsStriatal afferentsStriatal neuronsImmunoreactive fibersSubstance PLateral striatumDay 1StriatumPostnatal developmentBrain regionsNeuronsCompartmental expression
1995
Molecular Cloning of the Human Homolog of a Striatum-Enriched Phosphatase (STEP) Gene and Chromosomal Mapping of the Human and Murine Loci
Li X, Luna J, Lombroso P, Francke U. Molecular Cloning of the Human Homolog of a Striatum-Enriched Phosphatase (STEP) Gene and Chromosomal Mapping of the Human and Murine Loci. Genomics 1995, 28: 442-449. PMID: 7490079, DOI: 10.1006/geno.1995.1173.Peer-Reviewed Original ResearchConceptsSrc homology domain 3STEP geneTyrosine phosphataseSomatic cell hybrid analysisHuman fetal brain cDNA libraryFetal brain cDNA libraryPhosphatase catalytic domainCell hybrid analysisProtein tyrosine phosphataseAmino acid domainProline-rich regionCandidate disease genesBrain cDNA libraryUsher syndrome type 1CAmino acid levelsChromosomal mappingPhosphatase geneMutant lociHuman homologTrue homologsMolecular cloningCatalytic domainAcid domainMurine locusCDNA libraryIdentification of two alternatively spliced transcripts of STEP: a subfamily of brain-enriched protein tyrosine phosphatases
Sharma E, Zhao F, Bult A, Lombroso P. Identification of two alternatively spliced transcripts of STEP: a subfamily of brain-enriched protein tyrosine phosphatases. Brain Research 1995, 32: 87-93. PMID: 7494467, DOI: 10.1016/0169-328x(95)00066-2.Peer-Reviewed Original ResearchConceptsTyrosine phosphatase domainPhosphatase domainProtein tyrosineSpliced transcriptsExon-intron organizationProtein tyrosine phosphataseOpen reading frameTyrosine phosphataseReading frameDistinct functionsGenomic DNANorthern analysisSTEP geneSTEP isoformsMolecular massTranscriptsSTEP61ProteinMouse brainTyrosineCentral nervous systemSubfamiliesGenesNervous systemMonoclonal antibodiesCellular and molecular characterization of a brain-enriched protein tyrosine phosphatase
Boulanger L, Lombroso P, Raghunathan A, During M, Wahle P, Naegele. Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase. Journal Of Neuroscience 1995, 15: 1532-1544. PMID: 7869116, PMCID: PMC6577844, DOI: 10.1523/jneurosci.15-02-01532.1995.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAxonsBlotting, WesternBrainCerebral CortexCorpus StriatumImmunohistochemistryIn Situ HybridizationMiceMice, Inbred BALB CNeuronsPeptide FragmentsProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRNA, MessengerSynaptic TransmissionTissue DistributionConceptsSubstantia nigraAdult rat brainCombination of immunocytochemistrySitu hybridization studiesProjection neuronsBasal gangliaCaudate putamenPresynaptic axonsStriatal enriched protein tyrosine phosphataseRat brainBrain regionsImmunocytochemical stainingLesion experimentsWestern blotLesion studiesWestern blottingMonoclonal antibodiesMRNA expression patternsImmunoreactive formsImmunoreactive bandsProtein tyrosine phosphataseNigraSitu hybridizationHybridization studiesSTEP isoformsA Neuronal Protein Tyrosine Phosphatase Induced by Nerve Growth Factor (∗)
Sharma E, Lombroso P. A Neuronal Protein Tyrosine Phosphatase Induced by Nerve Growth Factor (∗). Journal Of Biological Chemistry 1995, 270: 49-53. PMID: 7814416, DOI: 10.1074/jbc.270.1.49.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceDNAEnzyme InductionIntracellular Signaling Peptides and ProteinsMolecular Sequence DataNerve Growth FactorsNerve Tissue ProteinsNeuronsPC12 CellsProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 7Recombinant Fusion ProteinsSequence Homology, Amino AcidConceptsNerve growth factorNGF treatmentGrowth factorNon-receptor protein tyrosine phosphataseRat brainNeuronal growthProtein tyrosine phosphataseMRNA levelsBrainNorthern blot analysisPC12 cellsBlot analysisTyrosine phosphataseTreatmentPhosphataseExpressionFusion proteinTyrosine phosphatase activity
1994
Protein tyrosine phosphatases in the nervous system.
Naegele J, Lombroso P. Protein tyrosine phosphatases in the nervous system. Critical Reviews In Neurobiology 1994, 9: 105-14. PMID: 8828006.Peer-Reviewed Original ResearchConceptsGrowth factor receptor signaling cascadesTyrosine kinaseReceptor signaling cascadesRole of PTPsNervous systemProtein tyrosineNeuronal developmentLevels of phosphotyrosineBrainEvidence pointsSignaling cascadesFunctional roleTyrosine phosphataseLocalization patternsNeurotransmittersImportant role
1993
A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures
Lombroso P, Naegele, Sharma E, Lerner M. A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures. Journal Of Neuroscience 1993, 13: 3064-3074. PMID: 8331384, PMCID: PMC6576687, DOI: 10.1523/jneurosci.13-07-03064.1993.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBasal GangliaBase SequenceBlotting, WesternBrainChromatography, AffinityCorpus StriatumDopamine and cAMP-Regulated Phosphoprotein 32FemaleGene ExpressionImmune SeraImmunohistochemistryKineticsMaleMolecular Sequence DataMolecular WeightNerve Tissue ProteinsNeuronsOligodeoxyribonucleotidesOligonucleotides, AntisenseOrgan SpecificityPhosphoproteinsPolymerase Chain ReactionProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsReceptors, DopamineRecombinant Fusion Proteins
1991
Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum.
Lombroso P, Murdoch G, Lerner M. Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 7242-7246. PMID: 1714595, PMCID: PMC52270, DOI: 10.1073/pnas.88.16.7242.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceAmino acid consensus sequenceAmino acid sequenceApparent molecular massRat striatal cDNA librarySingle geneVitro translationCDNA clonesStrong homologyCDNA libraryCytoplasmic membraneAcid sequenceRNA transcriptsN-terminusMolecular characterizationRNA analysisMolecular massAmino acidsProteinPhosphataseMRNASequenceHomologyGenesTerminus