2015
BDNF Induces Striatal-Enriched Protein Tyrosine Phosphatase 61 Degradation Through the Proteasome
Saavedra A, Puigdellívol M, Tyebji S, Kurup P, Xu J, Ginés S, Alberch J, Lombroso PJ, Pérez-Navarro E. BDNF Induces Striatal-Enriched Protein Tyrosine Phosphatase 61 Degradation Through the Proteasome. Molecular Neurobiology 2015, 53: 4261-4273. PMID: 26223799, PMCID: PMC4738169, DOI: 10.1007/s12035-015-9335-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrain-Derived Neurotrophic FactorCerebral CortexExtracellular Signal-Regulated MAP KinasesHippocampusMembrane PotentialsMiceNeostriatumNerve Growth FactorNeuronsNeurotrophin 3Phospholipase C gammaPhosphorylationProteasome Endopeptidase ComplexProtein Tyrosine Phosphatases, Non-ReceptorProteolysisReceptors, N-Methyl-D-AspartateUbiquitinationConceptsBrain-derived neurotrophic factorSTEP61 levelsCortical neuronsUbiquitin-proteasome systemStriatal-enriched protein tyrosine phosphatasePrimary cortical neuronsLevels/activitiesNerve growth factorNeurotrophic factorNeurotrophin-3Cultured striatalHippocampal neuronsCell depolarizationGrowth factorERK1/2 phosphorylationNeuronsStriatalTyrosine kinasePhospholipase C-gammaC gammaDifferent mechanismsLevelsBlockadeGluN2BProtein tyrosine phosphatase
2014
Inhibition of striatal‐enriched tyrosine phosphatase 61 in the dorsomedial striatum is sufficient to increased ethanol consumption
Darcq E, Hamida SB, Wu S, Phamluong K, Kharazia V, Xu J, Lombroso P, Ron D. Inhibition of striatal‐enriched tyrosine phosphatase 61 in the dorsomedial striatum is sufficient to increased ethanol consumption. Journal Of Neurochemistry 2014, 129: 1024-1034. PMID: 24588427, PMCID: PMC4055745, DOI: 10.1111/jnc.12701.Peer-Reviewed Original ResearchMeSH KeywordsAlcohol DrinkingAnimalsAntibodies, BlockingBlotting, WesternChoice BehaviorDown-RegulationEnzyme InhibitorsGene Knockdown TechniquesImmunohistochemistryLentivirusMaleMiceMice, Inbred C57BLMotor ActivityNeostriatumPhosphorylationProtein Tyrosine PhosphatasesQuinineRNA, Small InterferingSaccharin
2012
Calpain and STriatal-Enriched protein tyrosine Phosphatase (STEP) activation contribute to extrasynaptic NMDA receptor localization in a Huntington's disease mouse model
Gladding CM, Sepers MD, Xu J, Zhang LY, Milnerwood AJ, Lombroso PJ, Raymond LA. Calpain and STriatal-Enriched protein tyrosine Phosphatase (STEP) activation contribute to extrasynaptic NMDA receptor localization in a Huntington's disease mouse model. Human Molecular Genetics 2012, 21: 3739-3752. PMID: 22523092, PMCID: PMC3412376, DOI: 10.1093/hmg/dds154.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalpainCoculture TechniquesDisease Models, AnimalEnzyme ActivationEnzyme InhibitorsHuntington DiseaseIon Channel GatingMiceModels, BiologicalNeostriatumNeuronsPhosphorylationPhosphotyrosineProtein TransportProtein Tyrosine Phosphatases, Non-ReceptorReceptors, N-Methyl-D-AspartateSynapsesConceptsYAC128 striatumProtein tyrosine phosphatase activationNMDAR localizationCalpain cleavageProtein tyrosine phosphataseTyrosine phosphatase activationEarly synaptic defectsWhole-cell NMDAR currentsDisease mouse modelGluN2B expressionNMDA receptor traffickingMutant huntingtin proteinCalpain inhibitionTyrosine phosphataseHuntington's diseaseFull-length mhttPlasma membranePhosphatase activationC-terminusReceptor traffickingNMDAR traffickingPolyglutamine repeatsMouse modelHuntingtin proteinNMDA receptor localizationStriatal-Enriched Protein Tyrosine Phosphatase in Alzheimer’s Disease
Xu J, Kurup P, Nairn AC, Lombroso PJ. Striatal-Enriched Protein Tyrosine Phosphatase in Alzheimer’s Disease. Advances In Pharmacology 2012, 64: 303-325. PMID: 22840751, PMCID: PMC3740556, DOI: 10.1016/b978-0-12-394816-8.00009-x.Peer-Reviewed Original ResearchConceptsAlzheimer's diseaseNeurofibrillary tanglesStriatal-enriched protein tyrosine phosphataseAmyloid plaquesTreatment of ADHyperphosphorylated tau proteinSubstantial economic burdenProgressive diseasePotential clinical applicationsClinical symptomsBeta amyloidGlutamate receptorsEconomic burdenTau proteinCortical accumulationCognitive functionMemory lossBeneficial effectsDiseaseNeuronal membranesCommon formMultiple intracellularMillions of peopleClinical applicationImportant target