1998
Ca2+/calmodulin-dependent kinase II mediates simultaneous enhancement of gap-junctional conductance and glutamatergic transmission
Pereda A, Bell T, Chang B, Czernik A, Nairn A, Soderling T, Faber D. Ca2+/calmodulin-dependent kinase II mediates simultaneous enhancement of gap-junctional conductance and glutamatergic transmission. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 13272-13277. PMID: 9789078, PMCID: PMC23780, DOI: 10.1073/pnas.95.22.13272.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzylaminesCalciumCalcium ChlorideCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCell CommunicationDendritesEgtazic AcidElectric ConductivityElectric StimulationEnzyme ActivationEnzyme InhibitorsEvoked PotentialsExcitatory Postsynaptic PotentialsGap JunctionsGlutamic AcidGoldfishMembrane PotentialsNeuronsSpinal CordSulfonamidesSynapsesSynaptic TransmissionVestibulocochlear NerveConceptsGlutamatergic synapsesGap junctional conductanceCaM-KIIGap junctionsLong-term potentiationGoldfish Mauthner cellIntradendritic Ca2Intradendritic injectionPostsynaptic increaseExcitatory transmissionGlutamatergic transmissionAuditory afferentsSynaptic responsesSynaptic activityDependent kinase inhibitorDependent kinase IIIntracellular Ca2Interneuronal communicationSpecific peptide inhibitorChemical synapsesKinase inhibitorsMauthner cellKN-93Mammalian glutamatergic synapsesSynapses
1997
Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions
Sáez J, Nairn A, Czernik A, Fishman G, Spray D, Hertzberg E. Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions. Journal Of Molecular And Cellular Cardiology 1997, 29: 2131-2145. PMID: 9281445, DOI: 10.1006/jmcc.1997.0447.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornCalcium-Calmodulin-Dependent Protein KinasesCDC2 Protein KinaseCells, CulturedConnexin 43DNA, ComplementaryElectrophoresis, Gel, Two-DimensionalEnzyme InhibitorsGap JunctionsMyocardiumPatch-Clamp TechniquesPhosphorylationProtein Processing, Post-TranslationalRatsRecombinant Fusion ProteinsStaurosporineTetradecanoylphorbol AcetateConceptsProtein kinase CTwo-dimensional tryptic phosphopeptide mapsTryptic phosphopeptide mapsState of phosphorylationMyocyte gap junctionsProtein kinase inhibitorsGap junctionsMajor gap junction proteinPhosphorylation of connexin43Gap junction proteinPhosphopeptide mapsTryptic phosphopeptidesPKC-dependent mechanismFunctional couplingPhosphorylated formKinase CPhosphorylationNeonatal rat cardiocytesCx43 phosphorylationStaurosporineCellular distributionImmunoblot analysisRat cardiocytesJunction proteinsCx43Cardiac Myocytes Gap Junctions: Phosphorylation of CX43 through a Protein Kinase C-Dependent Pathway
Sáez J, Nairn A, Czernik A, Fishman G, Spray D, Hertzberg E. Cardiac Myocytes Gap Junctions: Phosphorylation of CX43 through a Protein Kinase C-Dependent Pathway. Series Of The Centro De Estudios Científicos 1997, 381-394. DOI: 10.1007/978-1-4899-1795-9_22.Peer-Reviewed Original Research
1990
Phosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II
SAEZ J, NAIRN A, CZERNIK A, SPRAY D, HERTZBERG E, GREENGARD P, BENNETT M. Phosphorylation of connexin 32, a hepatocyte gap‐junction protein, by cAMP‐dependent protein kinase, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II. The FEBS Journal 1990, 192: 263-273. PMID: 2170122, DOI: 10.1111/j.1432-1033.1990.tb19223.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesConnexinsElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelFemaleLiverMembrane ProteinsMolecular Sequence DataPeptide FragmentsPeptidesPhosphopeptidesPhosphorylationProtein Kinase CProtein KinasesRatsRats, Inbred StrainsConceptsProtein kinase CCAMP-dependent protein kinaseDependent protein kinase IIGap junction proteinPhosphopeptide mappingProtein kinaseSeryl residuesProtein kinase IICAMP-PKKinase IIKinase CCell typesConnexin 32PK IIPhosphoamino acid analysisDifferent gap junction proteinsSites of phosphorylationPhosphorylated synthetic peptideCAMP-PK activityGap junctionsAmino acid sequencingActivation of PKCDifferent cell typesPhysiological substratesSynthetic peptides