2014
Memory Enhancement by Targeting Cdk5 Regulation of NR2B
Plattner F, Hernández A, Kistler TM, Pozo K, Zhong P, Yuen EY, Tan C, Hawasli AH, Cooke SF, Nishi A, Guo A, Wiederhold T, Yan Z, Bibb JA. Memory Enhancement by Targeting Cdk5 Regulation of NR2B. Neuron 2014, 81: 1070-1083. PMID: 24607229, PMCID: PMC4010123, DOI: 10.1016/j.neuron.2014.01.022.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCells, CulturedCyclin-Dependent Kinase 5FemaleHippocampusMaleMemoryMemory DisordersMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataNeuronal PlasticityNeuronsOrgan Culture TechniquesPhosphorylationRatsRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateSynaptic TransmissionConceptsCell surface expressionReceptor cell surface expressionCyclin-dependent kinase 5Cdk5 regulationN-methyl-D-aspartate receptorsRegulatory mechanismsKinase 5NR2B functionSurface expressionNMDAR functionSubunit NR2BSynaptic plasticityEnhancerFundamental roleRegulationMemory formationNMDAR subunit NR2BCognitive enhancersValid treatment strategyPrime targetSynaptic transmissionNR2B phosphorylationNR2BPhosphorylationSurface level
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
Activation of Dopamine D4 Receptors Induces Synaptic Translocation of Ca2+/Calmodulin-Dependent Protein Kinase II in Cultured Prefrontal Cortical Neurons
Gu Z, Jiang Q, Yuen E, Yan Z. Activation of Dopamine D4 Receptors Induces Synaptic Translocation of Ca2+/Calmodulin-Dependent Protein Kinase II in Cultured Prefrontal Cortical Neurons. Molecular Pharmacology 2005, 69: 813-822. PMID: 16365279, DOI: 10.1124/mol.105.018853.Peer-Reviewed Original ResearchConceptsD4 receptor activationDependent protein kinase IIProtein kinase IIAlpha-CaMKIID4 receptorsDopamine D4 receptorCaMKII translocationKinase IIReceptor activationF-actinSynaptic translocationPostsynaptic sitesBinding of CaMKIITrisphosphate receptor/Ca2Receptor-mediated excitatory postsynaptic currentsAMPA receptor-mediated excitatory postsynaptic currentsPhospholipase C/inositolPrefrontal cortexCalmodulin binding siteExcitatory postsynaptic currentsGlutamate receptor 1 (GluR1) subunitPrefrontal cortical neuronsD4 receptor stimulationAutophosphorylation sitesSubcellular localization