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
2010
The Stress Hormone Corticosterone Increases Synaptic α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors via Serum- and Glucocorticoid-inducible Kinase (SGK) Regulation of the GDI-Rab4 Complex*
Liu W, Yuen EY, Yan Z. The Stress Hormone Corticosterone Increases Synaptic α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors via Serum- and Glucocorticoid-inducible Kinase (SGK) Regulation of the GDI-Rab4 Complex*. Journal Of Biological Chemistry 2010, 285: 6101-6108. PMID: 20051515, PMCID: PMC2825404, DOI: 10.1074/jbc.m109.050229.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Inflammatory AgentsCell LineCerebral CortexCorticosteroneGuanine Nucleotide Dissociation InhibitorsImmediate-Early ProteinsMiceNeuronsProtein Serine-Threonine KinasesProtein TransportRab4 GTP-Binding ProteinsRatsReceptors, AMPAReceptors, NeurotransmitterSynapsesUp-RegulationConceptsNucleotide Dissociation InhibitorSer-213Glucocorticoid-inducible kinaseRab proteinsKinase regulationDissociation inhibitorIsoxazolepropionic acid (AMPA) receptorsSmall GTPaseEarly endosomesAcid receptorsFunctional cycleCorticosteroid signalingSGK phosphorylationPlasma membraneRab4Receptor recyclingMolecular mechanismsCellular targetsCorticosteroid stress hormonesNeuronal functionPhosphorylationSurface expressionStress hormonesMembraneRegulation
2009
Assembly of a β2‐adrenergic receptor—GluR1 signalling complex for localized cAMP signalling
Joiner M, Lisé M, Yuen E, Kam A, Zhang M, Hall D, Malik Z, Qian H, Chen Y, Ulrich J, Burette A, Weinberg R, Law P, El‐Husseini A, Yan Z, Hell J. Assembly of a β2‐adrenergic receptor—GluR1 signalling complex for localized cAMP signalling. The EMBO Journal 2009, 29: 482-495. PMID: 19942860, PMCID: PMC2824466, DOI: 10.1038/emboj.2009.344.Peer-Reviewed Original ResearchMeSH KeywordsAdenylyl CyclasesAnimalsCalcium ChannelsCells, CulturedCerebral CortexCyclic AMP-Dependent Protein KinasesDisks Large Homolog 4 ProteinElectrophysiologyGene Expression RegulationGTP-Binding Protein alpha Subunits, GsHippocampusIntracellular Signaling Peptides and ProteinsMembrane ProteinsNeuronsRatsRats, Sprague-DawleyReceptors, Adrenergic, beta-2Receptors, AMPAConceptsUnknown molecular mechanismsMajor target proteinGluR1 surface expressionLocalized cAMPTarget proteinsMolecular mechanismsPhosphorylation of GluR1Selective regulationAdenylyl cyclaseProteinPSD-95PhosphorylationSurface expressionGlutamate receptor subunits GluR1PKAAssemblyPostsynaptic sitesCentral noradrenergic signalingHomologuesSubunit GluR1ComplexesCAMPSignalingAdrenergic receptorsStargazin