2024
Alternative translation initiation produces synaptic organizer proteoforms with distinct localization and functions
Lee P, Sun Y, Soares A, Fai C, Picciotto M, Guo J. Alternative translation initiation produces synaptic organizer proteoforms with distinct localization and functions. Molecular Cell 2024, 84: 3967-3978.e8. PMID: 39317199, PMCID: PMC11490368, DOI: 10.1016/j.molcel.2024.08.032.Peer-Reviewed Original ResearchTranslation initiation siteNeuronal pentraxin receptorAUG translational initiation siteAlternative translation initiation sitesN-terminal signal sequenceN-terminal transmembrane domainRNA secondary structureAlternative translation initiationN-terminal extensionTranslation initiationSignal sequenceProtein isoformsProtein localizationAUG initiatorTransmembrane domainWidespread mechanismSecondary structureInitiation siteAlternative usageAMPA-type glutamate receptorsProteoformsSecreted factorsProteinReduced AMPA receptorMRNA
2021
Sex Differences in the Ventral Tegmental Area and Nucleus Accumbens Proteome at Baseline and Following Nicotine Exposure
Lee AM, Mansuri MS, Wilson RS, Lam TT, Nairn AC, Picciotto MR. Sex Differences in the Ventral Tegmental Area and Nucleus Accumbens Proteome at Baseline and Following Nicotine Exposure. Frontiers In Molecular Neuroscience 2021, 14: 657064. PMID: 34335180, PMCID: PMC8317211, DOI: 10.3389/fnmol.2021.657064.Peer-Reviewed Original ResearchVentral tegmental areaC3H/HeJ miceGlial fibrillary acidic proteinChronic nicotine administrationNicotine administrationProtein abundanceProteomeIsobaric labelingNicotine exposureFemale miceTegmental areaHeJ miceNucleus accumbensNicotine addictionProteinSex differencesSample fractionationPathwayFibrillary acidic proteinTandem mass spectrometryNetwork analysisMouse strainsChronic nicotineMesolimbic systemNicotine reward
2020
Effects of nicotine on DARPP-32 and CaMKII signaling relevant to addiction
Lee AM, Picciotto MR. Effects of nicotine on DARPP-32 and CaMKII signaling relevant to addiction. Advances In Pharmacology 2020, 90: 89-115. PMID: 33706940, PMCID: PMC8008986, DOI: 10.1016/bs.apha.2020.09.002.Peer-Reviewed Original ResearchConceptsKey intracellular signaling cascadesIntracellular signaling cascadesDependent kinase IIPaul GreengardSignaling cascadesKinase IINicotine-dependent behaviorsNicotinic acetylcholine receptorsSecond messenger systemsNeuronal signalingInitial characterizationDARPP-32ProteinMessenger systemsAcetylcholine receptorsSignalingRoleCaMKIIGreengardNicotine addictionCascadeImmunohistochemical workDiscoveryReceptorsCAMP
2016
Evaluation of the Nicotinic Acetylcholine Receptor-Associated Proteome at Baseline and Following Nicotine Exposure in Human and Mouse Cortex
McClure-Begley TD, Esterlis I, Stone KL, Lam TT, Grady SR, Colangelo CM, Lindstrom JM, Marks MJ, Picciotto MR. Evaluation of the Nicotinic Acetylcholine Receptor-Associated Proteome at Baseline and Following Nicotine Exposure in Human and Mouse Cortex. ENeuro 2016, 3: eneuro.0166-16.2016. PMID: 27559543, PMCID: PMC4985585, DOI: 10.1523/eneuro.0166-16.2016.Peer-Reviewed Original ResearchConceptsPutative interacting proteinsQuantitative proteomic assessmentProtein-protein interactionsTemporal cortex tissueChaperone familyMood disordersInteracting proteinProtein complexesPresynaptic neurotransmitter releaseNovel etiological mechanismsNicotine exposureProteomic assessmentProteomeNicotinic acetylcholine receptorsMouse cortexProteinHigh-affinity nAChRsΒ2 subunitCortex of miceMaintenance of smokingNew treatment targetsResult of smokingNeurotransmitter releaseAcetylcholine receptorsPrimary function
2015
DARPP-32 interaction with adducin may mediate rapid environmental effects on striatal neurons
Engmann O, Giralt A, Gervasi N, Marion-Poll L, Gasmi L, Filhol O, Picciotto MR, Gilligan D, Greengard P, Nairn AC, Hervé D, Girault JA. DARPP-32 interaction with adducin may mediate rapid environmental effects on striatal neurons. Nature Communications 2015, 6: 10099. PMID: 26639316, PMCID: PMC4675091, DOI: 10.1038/ncomms10099.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBehavior, AnimalBrainCaffeineCalmodulin-Binding ProteinsCentral Nervous System StimulantsChlorocebus aethiopsCocaineCOS CellsDendritic SpinesDopamine and cAMP-Regulated Phosphoprotein 32EnvironmentFluorescence Recovery After PhotobleachingImmunoblottingImmunohistochemistryIn Vitro TechniquesMass SpectrometryMiceMice, Inbred C57BLMutationNeostriatumNeuronsNucleus AccumbensPhosphorylationRatsRats, Sprague-DawleyRewardConceptsAdducin phosphorylationCytoskeletal proteinsActin filamentsMolecular pathwaysCellular mechanismsEnvironmental changesPhosphorylationDARPP-32Striatal neuronsAdducinMutant miceSynaptic stabilityProteinCascadeMultiple effectsEnvironmental effectsBindsDendritic spinesNeuronsModification of responsesBrief exposurePathwayInteractionFilamentsEnrichment
2013
Exploring the Nicotinic Acetylcholine Receptor-Associated Proteome with iTRAQ and Transgenic Mice
McClure-Begley TD, Stone KL, Marks MJ, Grady SR, Colangelo CM, Lindstrom JM, Picciotto MR. Exploring the Nicotinic Acetylcholine Receptor-Associated Proteome with iTRAQ and Transgenic Mice. Genomics Proteomics & Bioinformatics 2013, 11: 207-218. PMID: 23891776, PMCID: PMC3806329, DOI: 10.1016/j.gpb.2013.05.005.Peer-Reviewed Original ResearchConceptsNicotinic acetylcholine receptorsPutative interacting proteinsΒ2 subunitMammalian central nervous systemAcetylcholine receptorsInteracting proteinProteomic analysisQuantitative proteomicsCytoskeletal rearrangementsIsobaric tagsNeuronal nicotinic acetylcholine receptorsCalcium signalingAbsolute quantitationΑ4β2 nAChRsProteinReduced expressionΒ2 subunit expressionPotential targetCentral nervous systemSubunitsExpressionPrincipal receptorTransgenic miceSubunit expressionΑ4
2009
The membrane cytoskeletal protein adducin is phosphorylated by protein kinase C in D1 neurons of the nucleus accumbens and dorsal striatum following cocaine administration
Lavaur J, Mineur YS, Picciotto MR. The membrane cytoskeletal protein adducin is phosphorylated by protein kinase C in D1 neurons of the nucleus accumbens and dorsal striatum following cocaine administration. Journal Of Neurochemistry 2009, 111: 1129-1137. PMID: 19780900, PMCID: PMC2810345, DOI: 10.1111/j.1471-4159.2009.06405.x.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsBenzazepinesBenzophenanthridinesCalmodulin-Binding ProteinsCocaineCorpus StriatumDopamine AntagonistsDopamine Uptake InhibitorsDose-Response Relationship, DrugEnzyme InhibitorsGene Expression RegulationGreen Fluorescent ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutNeuronsNucleus AccumbensPhosphorylationProtein Kinase CRacloprideReceptors, Dopamine D1Time FactorsConceptsProtein kinase CAdducin phosphorylationKinase CActin-binding proteinsFamily of proteinsPhosphorylation of adducinCytoskeletal protein adducinActin dynamicsCytoskeletal rearrangementsPhosphorylation stateCytoskeletal proteinsAdducinF-actinPhosphorylationNeuronal cytoskeletonCellular architectureProteinSynaptic functionMorphological changesCytoskeletonMedium spiny neuronsSpectrinRegimen of cocaineActinRegulation
2006
Nicotine‐Mediated Activation of Signal Transduction Pathways
Picciotto M. Nicotine‐Mediated Activation of Signal Transduction Pathways. Novartis Foundation Symposia 2006, 275: 83-95. DOI: 10.1002/9780470029237.ch7.ChaptersCyclic AMP response element binding proteinSignal transductionProtein phosphatase calcineurinSignal transduction pathwaysMAP kinase pathwayActivation of proteinsResponse element-binding proteinElement-binding proteinTranscription factorsPhosphatase calcineurinTransduction pathwaysProtein kinaseKinase pathwayNicotinic acetylcholine receptorsBinding proteinProteinTransductionAcetylcholine receptorsPathwayCalcium entryActivationLong-term changesSynaptic strengthCircuit-level changesKinase
2005
GalR1, but not GalR2 or GalR3, levels are regulated by galanin signaling in the locus coeruleus through a cyclic AMP‐dependent mechanism
Hawes JJ, Brunzell DH, Wynick D, Zachariou V, Picciotto MR. GalR1, but not GalR2 or GalR3, levels are regulated by galanin signaling in the locus coeruleus through a cyclic AMP‐dependent mechanism. Journal Of Neurochemistry 2005, 93: 1168-1176. PMID: 15934937, PMCID: PMC1352153, DOI: 10.1111/j.1471-4159.2005.03105.x.Peer-Reviewed Original ResearchConceptsCAMP-dependent mannerKnockout micePhysiological functionsCREB phosphorylationProtein levelsGALR1 expressionCell linesGalanin knockout miceMRNA levelsCAMP levelsMouse brainCyclic AMP-dependent mechanismGalR3Important rolePhosphorylationGalR1GalR2ProteinNegative feedbackMiceExpressionLevelsNucleusCATHImpaired Synaptic Plasticity and Learning in Mice Lacking β-Adducin, an Actin-Regulating Protein
Rabenstein RL, Addy NA, Caldarone BJ, Asaka Y, Gruenbaum LM, Peters LL, Gilligan DM, Fitzsimonds RM, Picciotto MR. Impaired Synaptic Plasticity and Learning in Mice Lacking β-Adducin, an Actin-Regulating Protein. Journal Of Neuroscience 2005, 25: 2138-2145. PMID: 15728854, PMCID: PMC1352335, DOI: 10.1523/jneurosci.3530-04.2005.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAvoidance LearningCalmodulin-Binding ProteinsConditioning, ClassicalCytoskeletonDendritesElectroshockFearFemaleFreezing Reaction, CatalepticGyrus CinguliHippocampusLearning DisabilitiesMaleMaze LearningMemory DisordersMiceMice, Inbred C57BLMice, KnockoutMice, Neurologic MutantsNerve Tissue ProteinsNeuronal PlasticityNucleus AccumbensRNA, MessengerConceptsBeta-adducinActin regulating proteinsCAMP-dependent mannerSynaptic plasticityActin cytoskeletonΒ-adducinCytoskeletal organizationPlasma membraneAdducinCellular mechanismsActivity-dependent synaptic plasticitySitu hybridizationPostsynaptic densityProteinPlasticitySpine morphologyImportant roleCytoskeletonSynaptic stimulationFamilyImpaired synaptic plasticityLong-term potentiationMiceMRNAHybridization
1988
Purification and characterization of PCPP‐260: A Purkinje cell‐enriched cyclic amp‐regulated membrane phosphoprotein of Mr 260,000
Weeks G, Picciotto M, Nairn A, Walaas S, Greengard P. Purification and characterization of PCPP‐260: A Purkinje cell‐enriched cyclic amp‐regulated membrane phosphoprotein of Mr 260,000. Synapse 1988, 2: 89-96. PMID: 2844000, DOI: 10.1002/syn.890020112.Peer-Reviewed Original ResearchConceptsCAMP-dependent protein kinaseMembrane proteinsProtein kinaseN-lauryl sarcosineIntegral membrane proteinsMajor tryptic phosphopeptidesPhosphoamino acid analysisTotal membrane proteinSodium dodecyl sulfate-polyacrylamide gel electrophoresisMembrane phosphoproteinDodecyl sulfate-polyacrylamide gel electrophoresisTryptic phosphopeptidesSulfate-polyacrylamide gel electrophoresisPossible functional roleProminent proteinsAlpha-methyl mannosideParticulate fractionMammalian cerebellumFunctional roleProteinPeptide mappingConcanavalin A-agaroseGel electrophoresisAcid analysisA-agarose