2005
Association/Dissociation of a Channel–Kinase Complex Underlies State-Dependent Modulation
Magoski NS, Kaczmarek LK. Association/Dissociation of a Channel–Kinase Complex Underlies State-Dependent Modulation. Journal Of Neuroscience 2005, 25: 8037-8047. PMID: 16135761, PMCID: PMC2873328, DOI: 10.1523/jneurosci.1903-05.2005.Peer-Reviewed Original ResearchConceptsProtein kinase CSrc homology 3 domainCation channelsSrc tyrosine kinasePKC-dependent modulationPhorbol esterSrc-dependent regulationAplysia bag cell neuronsBag cell neuronsProtein kinaseAssociated kinaseAssociation/dissociationEgg-laying hormonePhosphotyrosine stainingTyrosine kinaseKinase CKinaseReproductive behaviorNonselective cation channelsIon channelsChannel activityUnstimulated neuronsDependent modulationCell neuronsLong-term excitability
1991
Phosphorylation of membrane‐associated proteins by phorbol esters in isolated bag cell neurons of Aplysia
Azhderian E, Kaczmarek L. Phosphorylation of membrane‐associated proteins by phorbol esters in isolated bag cell neurons of Aplysia. Developmental Neurobiology 1991, 22: 105-115. PMID: 2030336, DOI: 10.1002/neu.480220202.Peer-Reviewed Original ResearchConceptsProtein kinase CBag cell neuronsKinase CPlasma membrane-containing fractionsProtein kinase C inhibitor H7Membrane-associated proteinsPhorbol esterExtent of phosphorylationMembrane-containing fractionsCell neuronsMembrane proteinsProtein phosphorylationNew speciesPhosphorylation statePlasma membraneTetradecanoyl phorbol 13Inhibitor H7Inactive phorbol esterIntact cellsPhosphate incorporationProtein extractsPhosphoproteinExtracellular mediumPhosphorylationProtein
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
1987
The role of protein kinase C in the regulation of ion channels and neurotransmitter release
Kaczmarek L. The role of protein kinase C in the regulation of ion channels and neurotransmitter release. Trends In Neurosciences 1987, 10: 30-34. DOI: 10.1016/0166-2236(87)90122-6.Peer-Reviewed Original ResearchProtein kinase CKinase CLipid environmentSecond messengerIntact cellsPhysiological activatorTypes of cellsAmount of neurotransmitterIon channelsChloride channelsPhorbol esterDiacylglycerolSynthetic diacylglycerolNeurotransmitter releaseEnzymeActivatorHormonal stimulationRegulationCellsImportant roleNervous systemNerve cellsMessengerActivityRole
1986
Phorbol Esters, Protein Phosphorylation and the Regulation of Neuronal Ion Channels
Kaczmarek L. Phorbol Esters, Protein Phosphorylation and the Regulation of Neuronal Ion Channels. Journal Of Experimental Biology 1986, 124: 375-392. PMID: 2428907, DOI: 10.1242/jeb.124.1.375.Peer-Reviewed Original ResearchConceptsProtein kinase CKinase CProtein kinase C resultsPhorbol esterNeuronal ion channelsProtein phosphorylationPlasma membraneLipid environmentIntact cellsIon channelsSuch activatorsEndogenous diacylglycerolVertebratesDiacylglycerolSynthetic diacylglycerolPhosphatidyl serineActivatorEndogenous electrical propertiesInactive speciesSynaptic transmissionInvertebratesCalcium channelsKinasePhosphorylationNervous system
1985
Enhancement 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