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
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
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
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