2012
An evolutionarily conserved mode of modulation of Shaw‐like K+ channels
Cotella D, Hernandez‐Enriquez B, Duan Z, Wu X, Gazula V, Brown MR, Kaczmarek LK, Sesti F. An evolutionarily conserved mode of modulation of Shaw‐like K+ channels. The FASEB Journal 2012, 27: 1381-1393. PMID: 23233530, PMCID: PMC3606535, DOI: 10.1096/fj.12-222778.Peer-Reviewed Original ResearchConceptsEffect of phosphorylationC. elegansACP-2Acid phosphataseMammalian homologMammalian homologueCaenorhabditis elegansMouse nervous systemRegulatory partnersBiochemical experimentsMolecular mechanismsElegansBehavioral defectsMode of modulationPhosphorylationPharmacological disruptionShaw familyMammalian brainSubset of neuronsVentricular zonePhosphataseModel systemNervous systemMice resultsElectrophysiological analysis
2006
Pharmacological activation and inhibition of Slack (Slo2.2) channels
Yang B, Gribkoff VK, Pan J, Damagnez V, Dworetzky SI, Boissard CG, Bhattacharjee A, Yan Y, Sigworth FJ, Kaczmarek LK. Pharmacological activation and inhibition of Slack (Slo2.2) channels. Neuropharmacology 2006, 51: 896-906. PMID: 16876206, DOI: 10.1016/j.neuropharm.2006.06.003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Infective Agents, LocalBepridilBithionolCalcium Channel BlockersCell Line, TransformedDose-Response Relationship, DrugDose-Response Relationship, RadiationElectric StimulationEnzyme ActivationEnzyme InhibitorsHumansMembrane PotentialsOocytesPatch-Clamp TechniquesPotassium Channels, Calcium-ActivatedQuinidineTransfectionXenopusConceptsSlack channelsConcentration-dependent mannerIschemic injuryPharmacological activationKNa channelsMammalian brainFiring ratePharmacological propertiesChannel subunitsReversible increaseChannel activityCell linesBepridilHEK cellsRobust activatorNeuronsStable cell linesInhibitionExcised patchesXenopus oocytesPresent studyBithionolChannel openingSpecific roleMembrane patches
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 ResearchConceptsProtein 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