2016
Disruption of Coordinated Presynaptic and Postsynaptic Maturation Underlies the Defects in Hippocampal Synapse Stability and Plasticity in Abl2/Arg-Deficient Mice
Xiao X, Levy AD, Rosenberg BJ, Higley MJ, Koleske AJ. Disruption of Coordinated Presynaptic and Postsynaptic Maturation Underlies the Defects in Hippocampal Synapse Stability and Plasticity in Abl2/Arg-Deficient Mice. Journal Of Neuroscience 2016, 36: 6778-6791. PMID: 27335408, PMCID: PMC4916252, DOI: 10.1523/jneurosci.4092-15.2016.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAnimalsAnimals, NewbornDendritic SpinesExcitatory Amino Acid AgentsFemaleGene Expression Regulation, DevelopmentalGlutamic AcidHippocampusHSP70 Heat-Shock ProteinsIn Vitro TechniquesMaleMiceMice, Inbred C57BLMice, KnockoutNeuronal PlasticityNeurotransmitter AgentsProtein-Tyrosine KinasesReceptors, GlutamateReceptors, N-Methyl-D-AspartateSubcellular FractionsSynapsesSynaptic PotentialsConceptsNMDA receptorsHippocampal synapsesEarly adulthoodFocal glutamate uncagingImmature glutamatergic synapsesDendritic spine numberNormal synaptic plasticityPostnatal day 21NMDA receptor currentsLate postnatal developmentHigh release probabilityArg kinaseForms of plasticityGlutamate uncagingSynapse lossPresynaptic sitesGlutamatergic synapsesSynapse stabilityPostsynaptic sitesSynaptic stabilityCultured neuronsMice ageReceptor currentsDay 21Synaptic plasticity
2010
Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function
Ko HS, Lee Y, Shin JH, Karuppagounder SS, Gadad BS, Koleske AJ, Pletnikova O, Troncoso JC, Dawson VL, Dawson TM. Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 16691-16696. PMID: 20823226, PMCID: PMC2944759, DOI: 10.1073/pnas.1006083107.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCell DeathCell LineDopamineGene Knockout TechniquesHumansIn Vitro TechniquesMiceMice, KnockoutMolecular Sequence DataMutationNeuronsParkinson DiseasePC12 CellsPhosphorylationProto-Oncogene Proteins c-ablRatsRecombinant Fusion ProteinsStress, PhysiologicalUbiquitinationUbiquitin-Protein LigasesConceptsParkinson's diseaseTreatment of PDSTI-571Postmortem PD brainsSporadic Parkinson's diseaseC-AblProtective functionNonreceptor tyrosine kinase c-AblMPTP intoxicationUbiquitin E3 ligase activityNeuroprotective approachesPD brainsSubstantia nigraDopaminergic neurotoxinProtective effectProtein type 2Subsequent neurotoxicityNervous systemType 2Parkin inactivationAutosomal recessive Parkinson's diseaseConditional knockoutKinase inhibitorsRecessive Parkinson's diseaseTyrosine kinase c-Abl
2004
Bidirectional Signaling Links the Abelson Kinases to the Platelet-Derived Growth Factor Receptor
Plattner R, Koleske AJ, Kazlauskas A, Pendergast AM. Bidirectional Signaling Links the Abelson Kinases to the Platelet-Derived Growth Factor Receptor. Molecular And Cellular Biology 2004, 24: 2573-2583. PMID: 14993293, PMCID: PMC355852, DOI: 10.1128/mcb.24.6.2573-2583.2004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineChemotaxisEnzyme ActivationIn Vitro TechniquesMacromolecular SubstancesMiceNIH 3T3 CellsPhospholipase C gammaPhosphorylationProtein-Tyrosine KinasesProto-Oncogene Proteins c-ablReceptor, Platelet-Derived Growth Factor alphaReceptor, Platelet-Derived Growth Factor betaRecombinant ProteinsSignal TransductionType C PhospholipasesConceptsPDGF beta receptorPlatelet-derived growth factorC-AblPLC-gamma1C-Abl nonreceptor tyrosine kinaseTyrosine kinaseGrowth factor signalsSrc family kinasesC-Abl functionNonreceptor tyrosine kinaseTyrosine kinase activityPlatelet-derived growth factor receptorAbundant phosphoinositideMembrane rufflingInducible complexNonredundant functionsFamily kinasesMembrane proteinsC-gamma1Factor signalsGrowth factor receptorAbelson kinaseKinase activityBiological processesChemotaxis defect
1995
Reduction of caveolin and caveolae in oncogenically transformed cells.
Koleske AJ, Baltimore D, Lisanti MP. Reduction of caveolin and caveolae in oncogenically transformed cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 1381-1385. PMID: 7877987, PMCID: PMC42523, DOI: 10.1073/pnas.92.5.1381.Peer-Reviewed Original ResearchConceptsPlasma membraneTransduction of signalsNIH 3T3 cellsSize of coloniesOncogenic transformationCaveolaeProtein coatCaveolinDemonstrated roleContact inhibitionCellular levelSoft agarElectron microscopy revealsCell linesCritical roleMicroscopy revealsCellsMembranePotocytosisTransductionFunctional alterationsOncogeneInvaginationColoniesRole