2005
Regulation of the timing of MNTB neurons by short-term and long-term modulation of potassium channels
Kaczmarek LK, Bhattacharjee A, Desai R, Gan L, Song P, von Hehn CA, Whim MD, Yang B. Regulation of the timing of MNTB neurons by short-term and long-term modulation of potassium channels. Hearing Research 2005, 206: 133-145. PMID: 16081004, DOI: 10.1016/j.heares.2004.11.023.Peer-Reviewed Original ResearchConceptsAnteroventral cochlear nucleusPotassium channelsAuditory pathwayAction potentialsCentral auditory pathwayVoltage-dependent potassium channelsMammalian auditory pathwayAmount of neurotransmitterProtein phosphorylationMNTB neuronsGene expressionBushy cellsPrincipal neuronsTrapezoid bodyCochlear nucleusIntrinsic excitabilityMedial nucleusVoltage-dependent channelsFiring patternsNeuronsAmplitude of currentsKv1 familySound stimuliLong-term modulationSound localization
1996
Regulation of potassium channels by protein kinases
Jonas E, Kaczmarek L. Regulation of potassium channels by protein kinases. Current Opinion In Neurobiology 1996, 6: 318-323. PMID: 8794088, DOI: 10.1016/s0959-4388(96)80114-0.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAnimalsCell MembraneEnzyme ActivationHumansKineticsPhosphorylationPotassium ChannelsProtein KinasesSerineThreonineTyrosine
1992
Recruitment of Ca2+ channels by protein kinase C during rapid formation of putative neuropeptide release sites in isolated Aplysia neurons
Knox R, Quattrocki E, Connor J, Kaczmarek L. Recruitment of Ca2+ channels by protein kinase C during rapid formation of putative neuropeptide release sites in isolated Aplysia neurons. Neuron 1992, 8: 883-889. PMID: 1316764, DOI: 10.1016/0896-6273(92)90202-o.Peer-Reviewed Original ResearchModulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes
Blumenthal E, Kaczmarek L. Modulation by cAMP of a slowly activating potassium channel expressed in Xenopus oocytes. Journal Of Neuroscience 1992, 12: 290-296. PMID: 1370322, PMCID: PMC6575684, DOI: 10.1523/jneurosci.12-01-00290.1992.Peer-Reviewed Original ResearchMeSH Keywords8-Bromo Cyclic Adenosine MonophosphateAmino Acid SequenceAnimalsCell MembraneCyclic AMPFemaleGene ExpressionHumansMembrane PotentialsMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedOocytesPhosphorylationPotassium ChannelsPotassium Channels, Voltage-GatedProgesteroneProtein Kinase InhibitorsProtein KinasesRatsRNATransfectionXenopus laevisConceptsMinK proteinCAMP-dependent protein kinasePotential phosphorylation sitesXenopus oocytesCAMP levelsPhosphorylation sitesProtein kinasePlasma membraneKinase activityChannel proteinsIntracellular cAMP levelsProtein inhibitorProteinKinasePotassium channelsOocytesVoltage-dependent potassium currentsIsK
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
1989
Protein kinase inhibitors selectively block phorbol ester- or forskolin- induced changes in excitability of Aplysia neurons
Conn P, Strong J, Azhderian E, Nairn A, Greengard P, Kaczmarek L. Protein kinase inhibitors selectively block phorbol ester- or forskolin- induced changes in excitability of Aplysia neurons. Journal Of Neuroscience 1989, 9: 473-479. PMID: 2537389, PMCID: PMC6569795, DOI: 10.1523/jneurosci.09-02-00473.1989.Peer-Reviewed Original ResearchConceptsProtein kinase CBag cell neuronsVoltage-dependent calcium currentsCAMP-PKPhorbol esterKinase CCell neuronsAction potentialsCalcium currentInhibitor of PKCProtein kinase inhibitorsPhorbol ester-induced enhancementKinase inhibitor 1Protein kinase inhibitor 1Adenylate cyclase activator forskolinCyclase activator forskolinProtein inhibitorGranule movementVoltage-dependent currentsCell action potentialsCAMP analogEffect of forskolinActivator forskolinPhorbol ester-induced changesNeuronal excitability
1988
The regulation of neuronal calcium and potassium channels by protein phosphorylation.
Kaczmarek L. The regulation of neuronal calcium and potassium channels by protein phosphorylation. 1988, 22: 113-38. PMID: 2852021.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
1986
Chapter 7 The role of protein kinases in the control of prolonged changes in neuronal excitability
Kaczmarek L, Strong J, Kauer J. Chapter 7 The role of protein kinases in the control of prolonged changes in neuronal excitability. Progress In Brain Research 1986, 69: 77-90. PMID: 3328878, DOI: 10.1016/s0079-6123(08)61050-x.Chapters
1985
Calcium/phosphatidylserine/diacylglycerol-dependent protein phosphorylation in the Aplysia nervous system
DeRiemer SA, Greengard P, Kaczmarek LK. Calcium/phosphatidylserine/diacylglycerol-dependent protein phosphorylation in the Aplysia nervous system. Journal Of Neuroscience 1985, 5: 2672-2676. PMID: 4045549, PMCID: PMC6565129, DOI: 10.1523/jneurosci.05-10-02672.1985.Peer-Reviewed Original ResearchMeSH KeywordsAplysiaCalciumDiglyceridesGlyceridesNerve Tissue ProteinsNervous SystemNeuronsPhosphatidylserinesPhosphorylationProtein KinasesConceptsProtein kinase CProtein kinase activityAplysia nervous systemBag cell neuronsKinase CProtein phosphorylationKinase activityDiacylglycerol-dependent protein kinaseEndogenous substrate proteinsEndogenous enzymesCytosolic fractionTumor-promoting phorbol diestersCell neuronsSubstrate proteinsCell clustersBag cell clustersProtein kinaseDalton proteinMammalian tissuesSpecific substratesNervous systemPhosphorylationBovine brainMammalian brainPolymixin B sulfateEnhancement of calcium current in Aplysia neurones by phorbol ester and protein kinase C
DeRiemer SA, Strong JA, Albert KA, Greengard P, Kaczmarek LK. Enhancement of calcium current in Aplysia neurones by phorbol ester and protein kinase C. Nature 1985, 313: 313-316. PMID: 2578617, DOI: 10.1038/313313a0.Peer-Reviewed Original ResearchConceptsProtein kinase CKinase CProtein kinase presentEndogenous protein kinase CKinase presentProtein kinase1Molecular mechanismsCellular componentsPhorbol ester TPAIon channelsPhorbol esterMammalian brainTumor-promoting phorbol ester TPAMollusc AplysiaPhysiological propertiesEnzymeNeuronal excitabilityDirect evidenceKinase1PhosphorylationProteinHigh concentrationsActivationAplysia
1982
Protein phosphorylation during afterdischarge in peptidergic neurons of Aplysia
Jennings K, Kaczmarek L, Hewick R, Dreyer W, Strumwasser F. Protein phosphorylation during afterdischarge in peptidergic neurons of Aplysia. Journal Of Neuroscience 1982, 2: 158-168. PMID: 6278103, PMCID: PMC6564306, DOI: 10.1523/jneurosci.02-02-00158.1982.Peer-Reviewed Original Research
1980
Microinjection of catalytic subunit of cyclic AMP-dependent protein kinase enhances calcium action potentials of bag cell neurons in cell culture
Kaczmarek LK, Jennings KR, Strumwasser F, Nairn AC, Walter U, Wilson FD, Greengard P. Microinjection of catalytic subunit of cyclic AMP-dependent protein kinase enhances calcium action potentials of bag cell neurons in cell culture. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 7487-7491. PMID: 6261262, PMCID: PMC350530, DOI: 10.1073/pnas.77.12.7487.Peer-Reviewed Original ResearchConceptsCalcium action potentialsBag cell neuronsAction potentialsCell neuronsInput resistanceCalcium antagonistsControl injectionsIntracellular injectionAbdominal ganglionPotassium channelsProtein kinaseNeuronsPrimary culturesInjected cellsInjectionIntracellular microinjectionMembrane potentialSubthreshold oscillationsAMP-dependent protein kinaseMicroinjectionCell culturesCyclic AMP-dependent protein kinaseSpike enhancementCatalytic subunitExtracellular medium