2011
Cellular Mechanisms for Dopamine D4 Receptor-induced Homeostatic Regulation of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors*
Yuen EY, Yan Z. Cellular Mechanisms for Dopamine D4 Receptor-induced Homeostatic Regulation of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors*. Journal Of Biological Chemistry 2011, 286: 24957-24965. PMID: 21622557, PMCID: PMC3137069, DOI: 10.1074/jbc.m111.221416.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Cells, CulturedDopamineExcitatory Amino Acid AgentsHomeostasisMembrane ProteinsMicrotubulesPyramidal CellsRatsRats, Sprague-DawleyReceptors, AMPAReceptors, Dopamine D4Signal TransductionConceptsGlutamatergic transmissionPFC neuronsPrefrontal cortexCalcium/calmodulin kinase II activityAMPAR responsesIsoxazolepropionic acid (AMPA) receptorsHomeostatic regulationCalmodulin kinase II activityAttention deficit hyperactivity disorderBi-directional regulationDopamine D4 receptorDeficit hyperactivity disorderAberrant dopaminePyramidal neuronsAMPA receptorsKinase II activitySynaptic currentsSynaptic targetingMental illnessAcid receptorsReceptor functionD4 receptorsCaMKII inhibitionActivity stateDistinct signaling mechanisms
2007
The Phosphorylation State of GluR1 Subunits Determines the Susceptibility of AMPA Receptors to Calpain Cleavage*
Yuen EY, Liu W, Yan Z. The Phosphorylation State of GluR1 Subunits Determines the Susceptibility of AMPA Receptors to Calpain Cleavage*. Journal Of Biological Chemistry 2007, 282: 16434-16440. PMID: 17428797, DOI: 10.1074/jbc.m701283200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCalpainCells, CulturedCerebral CortexEnzyme ActivationNeuronsPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Processing, Post-TranslationalProtein SubunitsRatsRats, Sprague-DawleyReceptors, AMPATime FactorsConceptsCalpain cleavagePhosphorylation stateProteolytic cleavageDependent protein kinase IITerminal fusion proteinEffect of phosphorylationProtein phosphatase 1/2AProtein kinase IIPhosphorylation sitesProtein kinaseCalpain cleavage sitesGluR1 subunitKinase IIFusion proteinActive CaMKIIAMPAR currentsCalpain regulationCleavage siteIsoxazoleproprionic acid (AMPA) receptorSubunitsIonotropic glutamate receptorsN-methyl-D-aspartate receptorsPhysiological studiesExcitatory synaptic transmissionAMPA receptor currents
2005
Serotonin 5-HT1A Receptors Regulate NMDA Receptor Channels through a Microtubule-Dependent Mechanism
Yuen EY, Jiang Q, Chen P, Gu Z, Feng J, Yan Z. Serotonin 5-HT1A Receptors Regulate NMDA Receptor Channels through a Microtubule-Dependent Mechanism. Journal Of Neuroscience 2005, 25: 5488-5501. PMID: 15944377, PMCID: PMC6724987, DOI: 10.1523/jneurosci.1187-05.2005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesDendritesExtracellular Signal-Regulated MAP KinasesIn Vitro TechniquesKinesinsMembrane PotentialsMicrotubulesMolecular Motor ProteinsNeuronsPatch-Clamp TechniquesPrefrontal CortexProtein SubunitsProtein TransportRatsReceptor, Serotonin, 5-HT1AReceptors, N-Methyl-D-AspartateSerotoninSerotonin 5-HT1 Receptor AgonistsSynapsesConceptsMicrotubule-dependent mechanismMEK/ERKNMDA receptorsPrefrontal cortexMicrotubule stabilityDendritic transportNMDAR interactionMicrotubule assemblyBiochemical evidenceMEK inhibitorsPFC pyramidal neuronsNMDA receptor channelsRole of serotoninCaMKIIERKNeuronal dendritesNMDAR functionMicrotubule stabilizerPathological conditionsPrimary targetReceptor channelsPyramidal neuronsNMDAR currentsSerotonin systemReceptors