2009
Ubiquitin-dependent lysosomal targeting of GABAA receptors regulates neuronal inhibition
Arancibia-Cárcamo I, Yuen E, Muir J, Lumb M, Michels G, Saliba R, Smart T, Yan Z, Kittler J, Moss S. Ubiquitin-dependent lysosomal targeting of GABAA receptors regulates neuronal inhibition. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 17552-17557. PMID: 19815531, PMCID: PMC2762659, DOI: 10.1073/pnas.0905502106.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCerebral CortexLeupeptinsLysosomesMicroscopy, ConfocalNeuronsProtein SubunitsRatsReceptors, GABA-ASynapsesUbiquitinConceptsSynaptic inhibitionGamma2 subunitInhibitory transmissionCerebral ischemiaAnoxic insultNeuronal inhibitionGABAA receptorsExcitatory currentsSynaptic sitesLysosomal targetingPathological conditionsLysosomal activityUnknown mechanismInhibitionReceptorsMolecular mechanismsIntracellular domainTargetingPathwayIschemiaNeuropathologyEndocytic pathwayInsult
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