2018
Evaluation of the Phosphoproteome of Mouse Alpha 4/Beta 2-Containing Nicotinic Acetylcholine Receptors In Vitro and In Vivo
Miller MB, Wilson RS, Lam TT, Nairn AC, Picciotto MR. Evaluation of the Phosphoproteome of Mouse Alpha 4/Beta 2-Containing Nicotinic Acetylcholine Receptors In Vitro and In Vivo. Proteomes 2018, 6: 42. PMID: 30326594, PMCID: PMC6313896, DOI: 10.3390/proteomes6040042.Peer-Reviewed Original ResearchProtein kinase APhosphorylation sitesPKA sitesHEK cellsNicotinic acetylcholine receptorsCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinase IIAcetylcholine receptorsKinase AKinase IIMouse brainSubunit phosphorylationNovel siteSubunitsAcute nicotine administrationΒ2 subunitMammalian brainCaMKIIPhosphorylationReceptor functionΑ4 subunitHuman brain tissueBeta 2Nicotine administration
2016
CaMKII Phosphorylation of TARPγ-8 Is a Mediator of LTP and Learning and Memory
Park J, Chávez AE, Mineur YS, Morimoto-Tomita M, Lutzu S, Kim KS, Picciotto MR, Castillo PE, Tomita S. CaMKII Phosphorylation of TARPγ-8 Is a Mediator of LTP and Learning and Memory. Neuron 2016, 92: 75-83. PMID: 27667007, PMCID: PMC5059846, DOI: 10.1016/j.neuron.2016.09.002.Peer-Reviewed Original ResearchConceptsCaMKII phosphorylation siteCaMKII substratePhosphorylation sitesDependent protein kinase IIProtein kinase IIReceptor-dependent activationNMDA receptor-dependent activationProtein phosphorylationAMPAR-mediated transmissionKinase IICaMKII-dependent enhancementLong-term potentiationCaMKII phosphorylationCellular mechanismsPhosphorylationMolecular targetsAMPA receptorsCrucial mediatorSynaptic plasticityMemory formationSynaptic insertionEssential stepSynaptic transmissionActivity-dependent strengtheningBasal transmission
2007
A Calcium- and Calmodulin-Dependent Kinase Iα/Microtubule Affinity Regulating Kinase 2 Signaling Cascade Mediates Calcium-Dependent Neurite Outgrowth
Uboha NV, Flajolet M, Nairn AC, Picciotto MR. A Calcium- and Calmodulin-Dependent Kinase Iα/Microtubule Affinity Regulating Kinase 2 Signaling Cascade Mediates Calcium-Dependent Neurite Outgrowth. Journal Of Neuroscience 2007, 27: 4413-4423. PMID: 17442826, PMCID: PMC6672303, DOI: 10.1523/jneurosci.0725-07.2007.Peer-Reviewed Original ResearchConceptsKinase domainNeurite outgrowthNeuronal differentiationCalmodulin-dependent kinase ITwo-hybridNeuro-2a cellsPhosphorylation sitesSignal transductionKinase ICaMKIKinase activityMicrotubule affinityKinase 2Calcium-dependent pathwayCritical regulatorIndependent screensPrimary hippocampal neuronsNovel siteCalcium ionophore ionomycinOutgrowthIonophore ionomycinSynaptic plasticityDifferentiationHippocampal neuronsPhysiological effects
2003
Identification and Characterization of AplysiaAdducin, an Aplysia Cytoskeletal Protein Homologous to Mammalian Adducins: Increased Phosphorylation at a Protein Kinase C Consensus Site during Long-Term Synaptic Facilitation
Gruenbaum LM, Gilligan DM, Picciotto MR, Marinesco S, Carew TJ. Identification and Characterization of AplysiaAdducin, an Aplysia Cytoskeletal Protein Homologous to Mammalian Adducins: Increased Phosphorylation at a Protein Kinase C Consensus Site during Long-Term Synaptic Facilitation. Journal Of Neuroscience 2003, 23: 2675-2685. PMID: 12684453, PMCID: PMC6742073, DOI: 10.1523/jneurosci.23-07-02675.2003.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAplysiaCalmodulin-Binding ProteinsCloning, MolecularConsensus SequenceCytoskeletal ProteinsHumansKineticsMammalsMiceModels, BiologicalMolecular Sequence DataMotor NeuronsNervous SystemNeuronal PlasticityNeuronsNeurons, AfferentPhosphorylationProtein Kinase CProtein Structure, TertiarySequence Homology, Amino AcidSerotoninSynaptic TransmissionConceptsMammalian adducinsProtein kinase CProtein kinase C consensus sitesLong-term facilitationPKC phosphorylation sitesAplysia nervous systemProtein HomologousPhosphorylation sitesConsensus sitesMembrane cytoskeletonRegulatory componentsCandidate proteinsLong-term synaptic facilitationKinase CAdducinAplysia homologIncreased phosphorylationPhosphorylationNervous system extractsAplysia neuronsShort-term facilitationParticulate fractionSynaptic alterationsMotor neuronsSynaptic transmission
2000
The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway
Paul S, Snyder G, Yokakura H, Picciotto M, Nairn A, Lombroso P. The Dopamine/D1 Receptor Mediates the Phosphorylation and Inactivation of the Protein Tyrosine Phosphatase STEP via a PKA-Dependent Pathway. Journal Of Neuroscience 2000, 20: 5630-5638. PMID: 10908600, PMCID: PMC6772528, DOI: 10.1523/jneurosci.20-15-05630.2000.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCatalytic DomainCorpus StriatumCyclic AMP-Dependent Protein KinasesEnzyme ActivationIn Vitro TechniquesMaleMolecular Sequence DataNeuronsPhosphoproteinsPhosphorus RadioisotopesPhosphorylationProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, Dopamine D1Signal TransductionConceptsProtein tyrosine phosphatase familyCAMP-dependent protein kinaseTryptic phosphopeptide mappingPotential phosphorylation sitesUnique N-terminalProtein-protein interactionsMembrane-associated proteinsRole of phosphorylationTyrosine phosphatase familyAmino acid sequenceSite-directed mutagenesisAmino acid sequencingPKA-dependent pathwayTyrosine phosphatase STEPPhosphatase familyPhosphopeptide mappingPhosphorylation sitesAlternative splicingSubcellular compartmentsProtein kinaseTerminal domainEquivalent residuesCytosolic proteinsSpecific residuesAcid sequence
1991
Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator.
Marshall J, Martin K, Picciotto M, Hockfield S, Nairn A, Kaczmarek L. Identification and localization of a dogfish homolog of human cystic fibrosis transmembrane conductance regulator. Journal Of Biological Chemistry 1991, 266: 22749-22754. PMID: 1718999, DOI: 10.1016/s0021-9258(18)54631-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell MembraneCloning, MolecularCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNADogfishHumansImmunoenzyme TechniquesMembrane ProteinsMolecular Sequence DataMolecular WeightProtein KinasesRectumSebaceous GlandsSequence Homology, Nucleic AcidSubstrate SpecificityConceptsCystic fibrosis transmembrane conductance regulatorHuman cystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorDogfish proteinRectal glandConductance regulatorPutative substrate sitesCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseMajor phosphorylation siteCyclic AMP-dependent protein phosphorylationApical plasma membraneAmino acid sequenceStudy of regulationPhosphorylation sitesProtein phosphorylationCDNA clonesProtein kinaseSimilar molecular massCFTR sequencePlasma membraneAcid sequenceImmunolocalization studiesMolecular mass