2000
Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains
Csanády L, Chan K, Seto-Young D, Kopsco D, Nairn A, Gadsby D. Severed Channels Probe Regulation of Gating of Cystic Fibrosis Transmembrane Conductance Regulator by Its Cytoplasmic Domains. The Journal Of General Physiology 2000, 116: 477-500. PMID: 10962022, PMCID: PMC2233695, DOI: 10.1085/jgp.116.3.477.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAdenylyl ImidodiphosphateAnimalsBase SequenceCyclic AMP-Dependent Protein KinasesCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNA PrimersFemaleHumansIn Vitro TechniquesIon Channel GatingModels, BiologicalMutationOocytesPhosphorylationProtein Structure, TertiaryRecombinant ProteinsXenopusConceptsR domainCFTR channelsPhosphorylated R domainWild-type CFTR channelsCytoplasmic regulatory domainCystic fibrosis transmembrane conductance regulatorNucleotide Binding DomainFibrosis transmembrane conductance regulatorDetailed functional characteristicsWT channelsApparent ATP affinityTransmembrane conductance regulatorCFTR Cl- channelPresence of PKANonhydrolyzable ATP analogue AMPPNPATP analogue AMPPNPATP bindingRegulatory domainCytoplasmic domainWt-CFTRBinding domainsGating eventsConductance regulatorATP affinityFunctional interaction
1999
Phosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase
Isohara T, Horiuchi A, Watanabe T, Ando K, Czernik A, Uno I, Greengard P, Nairn A, Suzuki T. Phosphorylation of the Cytoplasmic Domain of Alzheimer's β-Amyloid Precursor Protein at Ser655 by a Novel Protein Kinase. Biochemical And Biophysical Research Communications 1999, 258: 300-305. PMID: 10329382, DOI: 10.1006/bbrc.1999.0637.Peer-Reviewed Original ResearchConceptsNovel protein kinaseAlzheimer's beta-amyloid precursor proteinProtein kinase CExtracellular signal-regulated kinaseProtein kinaseCytoplasmic domainCalmodulin-dependent protein kinase IIΒ-amyloid precursor proteinPrecursor proteinAlzheimer's β-Amyloid Precursor ProteinSignal-regulated kinaseProtein kinase IIBeta-amyloid precursor proteinKinase IUnidentified proteinsKinase IIKinase CKinaseSer655ProteinAlzheimer's diseaseThr654Rat brainPhosphorylationDomainControl of CFTR Channel Gating by Phosphorylation and Nucleotide Hydrolysis
GADSBY D, NAIRN A. Control of CFTR Channel Gating by Phosphorylation and Nucleotide Hydrolysis. Physiological Reviews 1999, 79: s77-s107. PMID: 9922377, DOI: 10.1152/physrev.1999.79.1.s77.Peer-Reviewed Original ResearchConceptsNucleotide-binding domainCFTR channelsCytoplasmic nucleotide-binding domainsNucleotide hydrolysisChannel gatingDependent phosphorylation eventsCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelCFTR channel currentsCFTR channel gatingATP moleculesLarge cytoplasmic domainCommon lethal genetic diseaseSecond ATP moleculeSingle CFTR channelsATP hydrolysis cycleLethal genetic diseasePhosphorylation eventsGating cycleRegulatory domainCytoplasmic domainDifferent phosphoformsProgressive phosphorylationMultiple proteinsProtein productsHydrolysis cycle
1998
ATP hydrolysis cycles and the gating of CFTR Cl- channels.
Gadsby D, Dousmanis A, Nairn A. ATP hydrolysis cycles and the gating of CFTR Cl- channels. Acta Physiologica Scandinavica. Supplementum 1998, 643: 247-56. PMID: 9789567.Peer-Reviewed Original ResearchConceptsC-terminal nucleotideCFTR channelsAMP-PNPG proteinsN-terminal nucleotideCentral regulatory domainMore serine residuesProtein kinase ACFTR Cl- channelHydrolysis of ATPATP hydrolysis cycleCl- channelsGating cycleRegulatory domainCytoplasmic domainTight bindingSerine residuesHydrolyse ATPSecond ATPSequence homologyTransport proteinsKinase AOpen conformationAnalogues of ATPFunctional similarity
1997
Phosphorylation of Alzheimer β-Amyloid Precursor-like Proteins †
Suzuki T, Ando K, Isohara T, Oishi M, Lim G, Satoh Y, Wasco W, Tanzi R, Nairn A, Greengard P, Gandy S, Kirino Y. Phosphorylation of Alzheimer β-Amyloid Precursor-like Proteins †. Biochemistry 1997, 36: 4643-4649. PMID: 9109675, DOI: 10.1021/bi962618k.Peer-Reviewed Original ResearchConceptsAlzheimer's beta-amyloid precursor proteinCytoplasmic domain peptidePrecursor-like proteinsProtein kinase CCytoplasmic domainCultured cellsCell cycle-dependent mannerKinase CDomain peptideCycle-dependent mannerAmino acid sequenceHomologous amino acid sequencesGene familyKinase siteAcid sequenceExtracellular domainIntact cellsAPLP2Proteolytic processingAPLP1PhosphorylationPrecursor proteinProteinBeta-amyloid precursor proteinCdc2The Cytoplasmic Domain of Alzheimer’s Amyloid Precursor Protein Is Phosphorylated at Thr654, Ser655, and Thr668 in Adult Rat Brain and Cultured Cells
Oishi M, Nairn A, Czernik A, Lim G, Isohara T, Gandy S, Greengard P, Suzuki T. The Cytoplasmic Domain of Alzheimer’s Amyloid Precursor Protein Is Phosphorylated at Thr654, Ser655, and Thr668 in Adult Rat Brain and Cultured Cells. Molecular Medicine 1997, 3: 111-123. PMID: 9085254, PMCID: PMC2230054, DOI: 10.1007/bf03401803.Peer-Reviewed Original ResearchConceptsAlzheimer's disease amyloid precursor proteinCytoplasmic domainCultured cell linesCell cycle-dependent mannerAmyloid precursor proteinCultured cellsCycle-dependent mannerPhosphorylation state-specific antibodiesPhosphorylation-specific antibodiesPrecursor proteinCell linesProtein kinase C.Stoichiometric phosphorylationG2/M phaseAPP isoformsThr654Alzheimer amyloid precursor proteinOkadaic acidBiological functionsCell cycleKinase C.Intact cellsPhosphorylationHeLa cellsSpecific inhibitor
1996
387 Identification of a protein which interacts with the cytoplasmic domain of the Alzheimer amyloid protein Precursor
Watanabe T, Suzuki T, Sukegawa J, Sukegawa I, Nairn A, Greengard P. 387 Identification of a protein which interacts with the cytoplasmic domain of the Alzheimer amyloid protein Precursor. Neurobiology Of Aging 1996, 17: s97. DOI: 10.1016/s0197-4580(96)80389-7.Peer-Reviewed Original Research
1989
Identification of two protein kinases that phosphorylate the neural cell-adhesion molecule, N-CAM
Mackie K, Sorkin B, Nairn A, Greengard P, Edelman G, Cunningham B. Identification of two protein kinases that phosphorylate the neural cell-adhesion molecule, N-CAM. Journal Of Neuroscience 1989, 9: 1883-1896. PMID: 2542481, PMCID: PMC6569722, DOI: 10.1523/jneurosci.09-06-01883.1989.Peer-Reviewed Original ResearchConceptsProtein kinaseLarge polypeptidesCytoplasmic domainKinase ICell adhesion moleculeNeural cell adhesion moleculeThreonyl residuesCalmodulin-dependent protein kinase IN-CAMCalcium/calmodulin-dependent protein kinase ICyclic AMP-dependent protein kinaseCyclic GMP-dependent protein kinaseGlycogen synthase kinase-3AMP-dependent protein kinaseCommon phosphorylation sitesGMP-dependent protein kinaseCasein kinase IISynthase kinase-3Protein kinase IN-CAM polypeptidesChicken N-CAMProtein kinase CPrior phosphorylationPhosphorylation sitesAlternative splicing