2007
Cyclic AMP-dependent protein kinase and Epac mediate cyclic AMP responses in pancreatic acini
Chaudhuri A, Husain SZ, Kolodecik TR, Grant WM, Gorelick FS. Cyclic AMP-dependent protein kinase and Epac mediate cyclic AMP responses in pancreatic acini. AJP Gastrointestinal And Liver Physiology 2007, 292: g1403-g1410. PMID: 17234888, PMCID: PMC2975017, DOI: 10.1152/ajpgi.00478.2005.Peer-Reviewed Original ResearchConceptsProtein kinaseZymogen activationCAMP-dependent protein kinaseStimulation of PKACyclic AMP-dependent protein kinasePancreatic acinar cellsAMP-dependent protein kinaseApical actin cytoskeletonCAMP-binding proteinsRole of PKAMuscarinic agonist carbacholIntracellular zymogen activationSupraphysiological concentrationsCAMP-dependent pathwayActin cytoskeletonApical cytoskeletonPhenotypic responsesPKA responseAgonist carbacholCarbachol-induced activationAcinar cellsDecreased secretionEpacCAMP pathwayPancreatic acini
1999
Role of Calcineurin and Protein Phosphatase‐2A in the Regulation of DARPP‐32 Dephosphorylation in Neostriatal Neurons
Nishi A, Snyder G, Nairn A, Greengard P. Role of Calcineurin and Protein Phosphatase‐2A in the Regulation of DARPP‐32 Dephosphorylation in Neostriatal Neurons. Journal Of Neurochemistry 1999, 72: 2015-2021. PMID: 10217279, DOI: 10.1046/j.1471-4159.1999.0722015.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinCalcineurin InhibitorsCyclosporineDopamine and cAMP-Regulated Phosphoprotein 32Drug CombinationsDrug SynergismEnzyme InhibitorsIn Vitro TechniquesMaleMarine ToxinsMiceMice, Inbred C57BLNeostriatumNerve Tissue ProteinsNeuronsOkadaic AcidOxazolesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationProtein Phosphatase 1Protein Phosphatase 2ConceptsProtein phosphatase 1Protein phosphatase 2AOkadaic acidPhosphorylated DARPP-32DARPP-32 phosphorylationPhosphatase 2APP-2ADARPP-32Cyclic AMP-dependent protein kinaseAMP-dependent protein kinasePP-2A activityRole of calcineurinPhosphatase 1Calyculin AMouse neostriatal slicesProtein kinaseAction of cyclosporinDependent activationCalcineurinPresence of cyclosporinPhosphorylationDephosphorylationSynergistic increaseThr34Potent inhibitor
1996
Feedback modulation of ligand-engaged alpha L/beta 2 leukocyte integrin (LFA-1) by cyclic AMP-dependent protein kinase.
Rovere P, Inverardi L, Bender J, Pardi R. Feedback modulation of ligand-engaged alpha L/beta 2 leukocyte integrin (LFA-1) by cyclic AMP-dependent protein kinase. The Journal Of Immunology 1996, 156: 2273-9. PMID: 8690918, DOI: 10.4049/jimmunol.156.6.2273.Peer-Reviewed Original ResearchConceptsProtein kinase CAdhesion receptorsKinase CCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCytoskeletal anchoring proteinsIntegrin-dependent activationCAMP-dependent kinase activationIntracellular cAMP elevationCAMP elevationHeterologous cell linesLeukocyte integrinsAnchoring proteinsRegulated processProtein kinaseAdenylyl cyclase isoformsMolecular basisKinase activationIntercellular adhesionF-actinCell deadhesionHuman intercellular adhesion molecule-1LFA-1 receptorsDependent adhesionShort-term regulation
1995
Modulation of calcium currents by a D1 dopaminergic protein kinase/phosphatase cascade in rat neostriatal neurons
Surmeier D, Bargas J, Hemmings H, Nairn A, Greengard P. Modulation of calcium currents by a D1 dopaminergic protein kinase/phosphatase cascade in rat neostriatal neurons. Neuron 1995, 14: 385-397. PMID: 7531987, DOI: 10.1016/0896-6273(95)90294-5.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthine2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterAnimalsBrainCalcium Channel BlockersCalcium ChannelsCells, CulturedColforsinCyclic AMPCyclic AMP-Dependent Protein KinasesElectrophysiologyKineticsMembrane PotentialsNeostriatumNeuronsNifedipinePhosphoprotein PhosphatasesProtein Phosphatase 1RatsRats, WistarReceptors, Dopamine D1TetraethylammoniumTetraethylammonium CompoundsTime FactorsConceptsProtein phosphatase 1Protein kinaseInhibition of PP1Cyclic AMP-dependent protein kinaseAMP-dependent protein kinaseInhibition of PKARat neostriatal neuronsPhosphatase cascadePP1 activityReceptor-mediated activationPhosphatase 1Neostriatal neuronsCalcium currentPKA enhancementDifferential regulationHigh voltage-activated calcium currentsVoltage-activated calcium currentsWhole-cell voltage-clamp techniqueD1 pathwayMedium spiny neuronsCyclic AMP analogueD1 dopamine receptorsL-type currentDiversity of effectsSubset of neurons
1992
The protein kinase A-regulated cardiac CI− channel resembles the cystic fibrosis transmembrane conductance regulator
Nagel G, Hwang T, Nastiuk K, Nairn A, Gadsbyt D. The protein kinase A-regulated cardiac CI− channel resembles the cystic fibrosis transmembrane conductance regulator. Nature 1992, 360: 81-84. PMID: 1279437, DOI: 10.1038/360081a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBiological Transport, ActiveBlotting, NorthernChloride ChannelsChlorineCystic Fibrosis Transmembrane Conductance RegulatorGuanosine TriphosphateGuinea PigsIn Vitro TechniquesIon Channel GatingMembrane PotentialsMembrane ProteinsMyocardiumPhosphorylationProtein KinasesReceptors, Adrenergic, betaRNAConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorCyclic AMP-dependent protein kinaseAMP-dependent protein kinasePKA catalytic subunitResult of phosphorylationPhosphorylated channelsCatalytic subunitProtein kinaseSingle-channel conductanceNucleoside triphosphatesPhosphorylationMembrane potentialEpithelial cellsChannel activationRegulatorChannel conductanceCystic fibrosisKinaseCardiac ventricular myocytesSubunitsProteinUnitary current amplitudePhosphorylation 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 massSpk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine.
Stern DF, Zheng P, Beidler DR, Zerillo C. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. Molecular And Cellular Biology 1991, 11: 987-1001. PMID: 1899289, PMCID: PMC359764, DOI: 10.1128/mcb.11.2.987.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCell Cycle ProteinsCheckpoint Kinase 2Cloning, MolecularEscherichia coliFungal ProteinsGene LibraryGenes, FungalImmunoblottingMolecular Sequence DataProtein KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Nucleic AcidSerineSubstrate SpecificityThreonineTyrosineConceptsSerine/threonine kinaseProtein kinaseFusion proteinThreonine kinaseTyrosine phosphorylationGlutathione S-transferase fusion proteinCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseSerine protein kinaseSerine/threonineCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IITyrosine protein kinaseOpen reading frameProtein kinase IILambda gt11 libraryPutative kinaseNew kinasesThreonine phosphorylationCatalytic subunitSaccharomyces cerevisiaeBacterial proteinsReading frameAntiphosphotyrosine antibodyKinase II
1990
Nerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase
Brady M, Nairn A, Wagner J, Palfrey H. Nerve Growth Factor‐Induced Down‐Regulation of Calmodulin‐Dependent Protein Kinase III in PC12 Cells Involves Cyclic AMP‐Dependent Protein Kinase. Journal Of Neurochemistry 1990, 54: 1034-1039. PMID: 1689374, DOI: 10.1111/j.1471-4159.1990.tb02354.x.Peer-Reviewed Original ResearchConceptsWild-type cellsCalmodulin-dependent protein kinase IIICAMP-dependent protein kinase activityProtein kinase IIIProtein kinase activityEpidermal growth factorKinase IIIKinase activityA126-1B2 cellsCyclic AMP-dependent protein kinaseAMP-dependent protein kinasePC12 cellsNerve growth factorMutant PC12 cell lineElongation factor 2Growth factorAbility of NGFPC12 cell lineEffects of NGFProtein kinaseNGF additionA126-1B2Down regulationCell linesFactor 2
1989
Sequence and expression of chicken and mouse rsk: homologs of Xenopus laevis ribosomal S6 kinase.
Alcorta DA, Crews CM, Sweet LJ, Bankston L, Jones SW, Erikson RL. Sequence and expression of chicken and mouse rsk: homologs of Xenopus laevis ribosomal S6 kinase. Molecular And Cellular Biology 1989, 9: 3850-3859. PMID: 2779569, PMCID: PMC362446, DOI: 10.1128/mcb.9.9.3850.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChickensDNAGene Expression RegulationIn Vitro TechniquesMiceMolecular Sequence DataProtein BiosynthesisProtein KinasesRibosomal Protein S6Ribosomal Protein S6 KinasesRibosomal ProteinsRNA, MessengerSequence Homology, Nucleic AcidSpecies SpecificityTranscription, GeneticXenopus laevisConceptsRibosomal S6 kinaseMouse cDNAS6 kinaseCatalytic subunitKilobase pairsDistinct kinase domainsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseAmino acidsFamily of genesXenopus laevis cDNAIsolation of cDNAsPhosphorylase b kinaseExpression of chickenMRNA transcript sizeGenomic organizationXenopus proteinMolecular cloningMouse homologKinase domainProtein kinaseApparent molecular weightTranscript sizeB kinaseKinase geneSequence and Expression of Chicken and Mouse rsk: Homologs of Xenopus laevis Ribosomal S6 Kinase
Alcorta D, Crews C, Sweet L, Bankston L, Jones S, Erikson R. Sequence and Expression of Chicken and Mouse rsk: Homologs of Xenopus laevis Ribosomal S6 Kinase. Molecular And Cellular Biology 1989, 9: 3850-3859. DOI: 10.1128/mcb.9.9.3850-3859.1989.Peer-Reviewed Original ResearchRibosomal S6 kinaseMouse cDNAS6 kinaseCatalytic subunitKilobase pairsDistinct kinase domainsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseAmino acidsFamily of genesXenopus laevis cDNAIsolation of cDNAsPhosphorylase b kinaseExpression of chickenMRNA transcript sizeGenomic organizationXenopus proteinMolecular cloningMouse homologKinase domainProtein kinaseApparent molecular weightTranscript sizeB kinaseKinase geneMultisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. DOI: 10.1007/bf02918897.Peer-Reviewed Original ResearchCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sitesChloride conductance regulated by cyclic AMP-dependent protein kinase in cardiac myocytes
Bahinski A, Nairn A, Greengard P, Gadsby D. Chloride conductance regulated by cyclic AMP-dependent protein kinase in cardiac myocytes. Nature 1989, 340: 718-721. PMID: 2475783, DOI: 10.1038/340718a0.Peer-Reviewed Original ResearchConceptsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinaseChloride ion currentCatalytic subunitRegulatory proteinsKinase activationIon channelsKinaseChloride conductanceCalcium entrySingle-channel currentsCardiac myocytesCellsHeart cellsPhosphorylationAction potential repolarizationConductanceSubunitsProteinIntracellular dialysisMyocytesRegulationChannel currentsAdrenergic stimulationIdentification 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 splicingMultisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms
Ivar Walaas S, Nairn A. Multisite phosphorylation of microtubule-associated protein 2 (MAP-2) in rat brain: Peptide mapping distinguishes between cyclic AMP-, calcium/calmodulin-, and calcium/phospholipid-regulated phosphorylation mechanisms. Journal Of Molecular Neuroscience 1989, 1: 117-127. PMID: 2561875, DOI: 10.1007/bf02896895.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelMicrotubule-Associated ProteinsOrgan SpecificityPeptide MappingPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsConceptsCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIProtein kinaseCalcium/calmodulinProtein kinase IIKinase IICyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon phosphorylation sitesOnly serine residuesProtein 2Cyclic AMPMultisite phosphorylationThreonine residuesPhosphorylation sitesSerine residuesPhosphorylation systemPhosphorylation mechanismCytoskeletal proteinsMAP-2KinasePeptide mapsDistinct sites
1988
Neuromodulator‐Mediated Phosphorylation of Specific Proteins in a Neurotumor Hybrid Cell Line (NCB‐20)
Berry‐Kravis E, Kazmierczak B, Derechin V, Dawson G. Neuromodulator‐Mediated Phosphorylation of Specific Proteins in a Neurotumor Hybrid Cell Line (NCB‐20). Journal Of Neurochemistry 1988, 50: 1287-1296. PMID: 2450174, DOI: 10.1111/j.1471-4159.1988.tb10606.x.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthine2-ChloroadenosineAdenosineAlprostadilAnimalsBrainCalcimycinColforsinCricetinaeCyclic AMPElectrophoresis, Polyacrylamide GelEmbryo, MammalianEnkephalin, LeucineEnkephalin, Leucine-2-AlanineHybrid CellsImmunoassayMiceNerve Tissue ProteinsNeuroblastomaNeurotransmitter AgentsPhosphoproteinsPhosphorylationProtein KinasesSerotoninTumor Cells, CulturedTyrosine 3-MonooxygenaseConceptsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCalcium/phospholipid-dependent protein kinasePhospholipid-dependent protein kinaseProtein kinaseHybrid cell linesCalcium/phospholipid-dependent kinaseCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinasePC12 cellsStimulation of phosphorylationPhospholipid-dependent kinaseCell linesDifferentiated PC12 cellsMajor synaptic proteinsUnique proteinsSpecific proteinsMajor proteinsKinasePhosphorylationCyclic AMP-dependent protein kinase opens chloride channels in normal but not cystic fibrosis airway epithelium
Li M, McCann J, Liedtket C, Nairn A, Greengard P, Welsh M. Cyclic AMP-dependent protein kinase opens chloride channels in normal but not cystic fibrosis airway epithelium. Nature 1988, 331: 358-360. PMID: 2448645, DOI: 10.1038/331358a0.Peer-Reviewed Original ResearchConceptsCAMP-dependent protein kinaseProtein kinaseRegulatory proteinsCl- channelsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon lethal genetic diseaseNormal cellsLethal genetic diseaseApical Cl- channelsCatalytic subunitCell-free patchesCystic fibrosis airway epitheliaGenetic diseasesVariety of hormonesCF airway epitheliaCF cellsChloride channelsKinaseIntracellular levelsProteinAirway epitheliumCyclic AMPChloride secretionCells
1987
Stimulation of protein kinase C recruits covert calcium channels in Aplysia bag cell neurons
Strong J, Fox A, Tsien R, Kaczmarek L. Stimulation of protein kinase C recruits covert calcium channels in Aplysia bag cell neurons. Nature 1987, 325: 714-717. PMID: 2434853, DOI: 10.1038/325714a0.Peer-Reviewed Original ResearchConceptsProtein kinase CBag cell neuronsKinase CProtein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseAplysia bag cell neuronsCell neuronsCalcium channelsSingle-channel levelExcitable cellsKinaseUntreated cellsUnitary conductanceCalcium currentPeptidergic bag cell neuronsVoltage-activated calcium channelsCardiac muscleDifferent unitary conductancesCellsDifferent mechanismsVoltage-activated calcium currentsChannel levelSecond classNeurons
1986
Protein phosphorylation in cultured endothelial cells
Mackie K, Lai Y, Nairn A, Greengard P, Pitt B, Lazo J. Protein phosphorylation in cultured endothelial cells. Journal Of Cellular Physiology 1986, 128: 367-374. PMID: 3745280, DOI: 10.1002/jcp.1041280304.Peer-Reviewed Original ResearchConceptsCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinase activityProtein kinaseKinase activityCyclic GMP-dependent protein kinase activityRespective substrate proteinsProtein phosphorylation systemsProtein kinase CSubstrate proteinsProtein phosphorylationPhosphorylation systemEndothelial cellsNumerous substratesTyrosine kinaseKinase CPulmonary artery endothelial cellsKinaseCultured endothelial cellsArtery endothelial cellsSimilar culture conditionsCulture conditionsCells
1983
GABAergic synapses supramolecular organization and biochemical regulation
Guidotti A, Corda MG, Wise BC, Vaccarino F, Costa E. GABAergic synapses supramolecular organization and biochemical regulation. Neuropharmacology 1983, 22: 1471-1479. PMID: 6322041, DOI: 10.1016/0028-3908(83)90115-6.Peer-Reviewed Original ResearchConceptsProtein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseBasic proteinDependent protein kinaseCyclic AMP-dependent phosphorylationRecognition sitesGABA-modulinMyelin basic proteinAmino acid compositionBiochemical regulationMolecular mechanismsHigh-affinity bindingPostsynaptic neuronal membranesProtein
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