2007
Nicotine‐induced phosphorylation of ERK in mouse primary cortical neurons: evidence for involvement of glutamatergic signaling and CaMKII
Steiner RC, Heath CJ, Picciotto MR. Nicotine‐induced phosphorylation of ERK in mouse primary cortical neurons: evidence for involvement of glutamatergic signaling and CaMKII. Journal Of Neurochemistry 2007, 103: 666-678. PMID: 17666046, DOI: 10.1111/j.1471-4159.2007.04799.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCalcium-Calmodulin-Dependent Protein Kinase Type 2Cells, CulturedCerebral CortexCulture MediaDose-Response Relationship, DrugExtracellular Signal-Regulated MAP KinasesFemaleGlutamic AcidIndicators and ReagentsMiceMice, Inbred C57BLMice, KnockoutNeuronsNicotineNicotinic AgonistsPhosphorylationPregnancyReceptors, GlutamateReceptors, NicotinicReverse Transcriptase Polymerase Chain ReactionSignal TransductionSynaptic TransmissionConceptsNicotine-induced ERK phosphorylationExtracellular signal-regulated kinaseERK phosphorylationCAMP-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IINicotinic acetylcholine receptor inhibitorNicotine-induced phosphorylationSignal-regulated kinaseCortical neuronsProtein kinase IIProtein kinase CMouse primary cortical neuronsKinase II activityAlpha3/beta4Calmodulin-dependent protein kinase II activityGlutamatergic signalingProtein kinaseVoltage-gated sodium channelsKinase IICultured mouse cortical neuronsKinase CCalcium/calmodulin-dependent protein kinase II activityPhosphorylationL-type voltage-gated calcium channels
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
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
1996
Structure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I
Picciotto M, Nastiuk K, Nairn A. Structure, Regulation, and Function of Calcium/Calmodulin-Dependent Protein Kinase I. Advances In Pharmacology 1996, 36: 251-275. PMID: 8783563, DOI: 10.1016/s1054-3589(08)60585-2.Peer-Reviewed Original ResearchConceptsProtein kinaseProtein kinase CMyosin light chain kinaseKinase ICaM kinaseSecond messenger-regulated protein kinasesCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase ICAMP-dependent protein kinaseSpecific subcellular locationsMultifunctional protein kinaseTerminal regulatory domainDependent protein kinaseCaM kinase familyClass of enzymesProtein kinase ICaM kinase IAmino acid residuesMyosin P-light chainDomain bindsAutoinhibitory mechanismRegulatory domainKinase familyProtein phosphorylationLight chain kinase
1995
The Regulatory Region of Calcium/Calmodulin-dependent Protein Kinase I Contains Closely Associated Autoinhibitory and Calmodulin-binding Domains (∗)
Yokokura H, Picciotto M, Nairn A, Hidaka H. The Regulatory Region of Calcium/Calmodulin-dependent Protein Kinase I Contains Closely Associated Autoinhibitory and Calmodulin-binding Domains (∗). Journal Of Biological Chemistry 1995, 270: 23851-23859. PMID: 7559563, DOI: 10.1074/jbc.270.40.23851.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesCalmodulinDNA, ComplementaryEnzyme InhibitorsIn Vitro TechniquesMolecular Sequence DataMutagenesisMyosin-Light-Chain KinaseRatsRecombinant Fusion ProteinsSequence DeletionSequence Homology, Amino AcidStructure-Activity RelationshipConceptsCaM kinase IKinase IProtein kinase ITruncation mutantsCalmodulin-dependent protein kinase ICalcium/calmodulin-dependent protein kinase IDependent protein kinase IDependent protein kinaseSyntide-2Active kinaseAutoinhibitory domainDependent activityGlutathione S-transferaseProtein kinaseRegulatory regionsActive mutantMutantsFusion proteinPeptide substratesIntrasteric mechanismGlutathione-Sepharose 4B.COOH-terminalS-transferaseImmunochemical localization of calcium/calmodulin‐dependent protein kinase I
Picciotto M, Zoli M, Bertuzzi G, Nairn A. Immunochemical localization of calcium/calmodulin‐dependent protein kinase I. Synapse 1995, 20: 75-84. PMID: 7624832, DOI: 10.1002/syn.890200111.Peer-Reviewed Original ResearchConceptsKinase IProtein kinase ICaM kinase INon-neuronal tissuesImmunoreactive speciesCalmodulin-dependent protein kinase IGlutathione S-transferase fusion proteinCalcium/calmodulin-dependent protein kinase IRat brainDependent protein kinase ISubcellular fractionation studiesRecombinant kinasesRat brain enzymeNeuronal cell bodiesCytosolic localizationProtein kinaseMultiple immunoreactive speciesMajor immunoreactive speciesFusion proteinMultiple neuronal processesWidespread cellMajor immunoreactive bandRat cDNAPrimary structureSynapsin I.
1994
Calcium/calmodulin-dependent protein kinases.
Nairn AC, Picciotto MR. Calcium/calmodulin-dependent protein kinases. Seminars In Cancer Biology 1994, 5: 295-303. PMID: 7803766.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein Kinase Type 4Calcium-Calmodulin-Dependent Protein KinasesElongation Factor 2 KinaseHumansMolecular Sequence DataMyosin-Light-Chain KinasePhosphorylationConceptsProtein kinaseSecond messenger-regulated protein kinasesCaM-dependent protein kinaseEssential intracellular second messengerEF-2 kinaseCaM kinase ICaM kinase IVCaM kinase IIIntracellular second messengerMyosin light chain kinaseEukaryotic systemsProtein phosphorylationKinase ILight chain kinaseKinase IIPhosphorylase kinaseGene expressionKinase IVSecond messengerKinaseChain kinaseImportant familyCell proliferationNeurotransmitter releaseRegulation
1993
Calcium/calmodulin-dependent protein kinase I. cDNA cloning and identification of autophosphorylation site.
Picciotto MR, Czernik AJ, Nairn AC. Calcium/calmodulin-dependent protein kinase I. cDNA cloning and identification of autophosphorylation site. Journal Of Biological Chemistry 1993, 268: 26512-26521. PMID: 8253780, DOI: 10.1016/s0021-9258(19)74343-9.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal GlandsAmino Acid SequenceAnimalsBase SequenceBinding SitesBrainCalcium-Calmodulin-Dependent Protein Kinase Type 1Calcium-Calmodulin-Dependent Protein KinasesCattleCloning, MolecularDNA, ComplementaryEscherichia coliLiverLungMolecular Sequence DataPhosphorylationRatsRNA, MessengerSequence Homology, Amino AcidConceptsCaM kinase IKinase IProtein kinaseCatalytic domainThreonyl residuesFusion proteinGlutathione S-transferase fusion proteinS-transferase fusion proteinCAMP-dependent protein kinaseDependent protein kinase IComplete amino acid sequenceBovine brain cDNA libraryInvariant amino acidsAmino acidsSynapsin IAmino acid sequenceBrain cDNA libraryClass of enzymesSynaptic vesicle proteinsProtein kinase ICaM kinase IIAutophosphorylation sitesRNase protection assaysSingle geneCDNA library
1992
Phosphorylation of the cystic fibrosis transmembrane conductance regulator.
Picciotto MR, Cohn JA, Bertuzzi G, Greengard P, Nairn AC. Phosphorylation of the cystic fibrosis transmembrane conductance regulator. Journal Of Biological Chemistry 1992, 267: 12742-12752. PMID: 1377674, DOI: 10.1016/s0021-9258(18)42339-3.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorProtein kinase CFibrosis transmembrane conductance regulatorProtein kinaseTransmembrane conductance regulatorR domainRegulation of CFTRCalmodulin-dependent protein kinase IConductance regulatorCalcium/calmodulin-dependent protein kinase IDirect amino acid sequencingCyclic AMP-dependent protein kinaseCyclic GMP-dependent protein kinaseAMP-dependent protein kinaseGMP-dependent protein kinaseCF 2Peptide mappingProtein kinase IAmino acid sequencingDifferent second messenger pathwaysSecond messenger pathwaysDirect phosphorylationKinase ISerine 660Seryl residues
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
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