2000
Regulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo
Snyder G, Allen P, Fienberg A, Valle C, Huganir R, Nairn A, Greengard P. Regulation of Phosphorylation of the GluR1 AMPA Receptor in the Neostriatum by Dopamine and Psychostimulants In Vivo. Journal Of Neuroscience 2000, 20: 4480-4488. PMID: 10844017, PMCID: PMC6772453, DOI: 10.1523/jneurosci.20-12-04480.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzazepinesCentral Nervous System StimulantsDopamineDopamine and cAMP-Regulated Phosphoprotein 32In Vitro TechniquesMaleMethamphetamineMiceMice, Inbred C57BLMice, KnockoutMicrowavesNeostriatumNerve Tissue ProteinsOkadaic AcidPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1Protein Phosphatase 2Receptors, AMPAReceptors, Dopamine D1Receptors, Dopamine D2Recombinant Fusion ProteinsSerineConceptsCAMP-dependent protein kinaseProtein phosphatase 2A.AMPA-type glutamate receptorsCalmodulin-dependent kinase IICalcium/calmodulin-dependent kinase IIRegulation of phosphorylationProtein kinase CPhosphatase 2A.Protein kinaseKinase IIPhosphorylation of GluR1Kinase CGluR1 AMPA receptorsPhosphorylationCellular effectorsGlutamate receptorsDARPP-32Physiological activityAMPA receptorsPsychostimulant cocaineChannel conductanceReceptorsD1-type dopamine receptorsActivationVivo
1999
Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin
Yan Z, Hsieh–Wilson L, Feng J, Tomizawa K, Allen P, Fienberg A, Nairn A, Greengard P. Protein phosphatase 1 modulation of neostriatal AMPA channels: regulation by DARPP–32 and spinophilin. Nature Neuroscience 1999, 2: 13-17. PMID: 10195174, DOI: 10.1038/4516.Peer-Reviewed Original ResearchConceptsPP-1Protein phosphatase 1DARPP-32Distinct molecular mechanismsPhosphatase 1Molecular mechanismsAMPA receptor-mediated synaptic transmissionPostsynaptic densityAMPA channelsRegulationSynaptic plasticitySpinophilinNeostriatal neuronsPlasticityPhysiological evidenceGlutamate channelsSynaptic transmissionAMPA receptorsPhosphoproteinProteinMechanismBindingActivityModulationCatalytic activity
1997
Glutamate-Dependent Phosphorylation of Elongation Factor-2 and Inhibition of Protein Synthesis in Neurons
Marin P, Nastiuk K, Daniel N, Girault J, Czernik A, Glowinski J, Nairn A, Prémont J. Glutamate-Dependent Phosphorylation of Elongation Factor-2 and Inhibition of Protein Synthesis in Neurons. Journal Of Neuroscience 1997, 17: 3445-3454. PMID: 9133370, PMCID: PMC6573691, DOI: 10.1523/jneurosci.17-10-03445.1997.Peer-Reviewed Original ResearchMeSH Keywords6-Cyano-7-nitroquinoxaline-2,3-dioneAnimalsAntibody SpecificityCalciumCell SurvivalCells, CulturedCerebral CortexDizocilpine MaleateExcitatory Amino Acid AntagonistsGlutamic AcidMiceNerve Tissue ProteinsNeuronsNeurotoxinsPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationProtein BiosynthesisProtein Synthesis InhibitorsReceptors, AMPAReceptors, N-Methyl-D-AspartateConceptsNeuronal deathEukaryotic elongation factor 2Factor 2Cortical neuronsElongation factor 2Glutamate receptorsProtective effectLong-term effectsProtein synthesisPersistent inhibitionPharmacological analysisPharmacological inhibitionCytosolic Ca2Phosphorylation state-specific antibodiesNeuronsNMDAGlutamateInhibitionProtein translationDeathPhosphorylationClose correlationTransient phosphorylationCa2Excitotoxicity