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
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-transferase
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
1985
Aplysia neurons express a gene encoding multiple FMRFamide neuropeptides
Schaefer M, Picciotto M, Kreiner T, Kaldany R, Taussig R, Scheller R. Aplysia neurons express a gene encoding multiple FMRFamide neuropeptides. Cell 1985, 41: 457-467. PMID: 3838698, DOI: 10.1016/s0092-8674(85)80019-2.Peer-Reviewed Original ResearchConceptsAlternate RNA splicingAplysia nervous systemLys-Arg residuesHaploid genomeFMRFamide neuropeptidesRNA splicingCDNA clonesAnimal kingdomCDNA libraryMultiple transcriptsSingle copyCarboxy terminusAmino terminusInvertebrate tissuesFMRFamide peptidesDifferent tissuesPrecursor proteinPeptide Phe-MetGenesTerminusAplysia neuronsResiduesPhe-MetVariety of effectsArg-Phe