2009
Maitotoxin converts the plasmalemmal Ca2+ pump into a Ca2+-permeable nonselective cation channel
Sinkins W, Estacion M, Prasad V, Goel M, Shull G, Kunze D, Schilling W. Maitotoxin converts the plasmalemmal Ca2+ pump into a Ca2+-permeable nonselective cation channel. American Journal Of Physiology - Cell Physiology 2009, 297: c1533-c1543. PMID: 19794142, PMCID: PMC2793065, DOI: 10.1152/ajpcell.00252.2009.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsAnimals, Genetically ModifiedCalciumCation Transport ProteinsCationsCell MembraneCells, CulturedDown-RegulationElectric ConductivityFibroblastsHumansIon ChannelsKidneyMarine ToxinsMiceOxocinsPermeabilityPlasma Membrane Calcium-Transporting ATPasesRNA, Small InterferingSpodopteraUp-RegulationConceptsPermeable nonselective cation channelNonselective cation channelsCation channelsSpodoptera frugiperda (Sf9) insect cellsHEK cellsMouse embryonic fibroblastsHuman embryonic kidney 293 cellsEmbryonic kidney 293 cellsKidney 293 cellsInsect cellsEmbryonic fibroblastsWhole-cell membrane currentsMolecular identityCell membrane currentsCell typesPMCACytosolic freeMarine toxinsEnhanced expressionWhole-cell currentsPlasmalemmal Ca2PalytoxinATPaseCellsMaitotoxin
2001
Regulation of Drosophila transient receptor potential‐like (TrpL) channels by phospholipase C‐dependent mechanisms
Estacion M, Sinkins W, Schilling W. Regulation of Drosophila transient receptor potential‐like (TrpL) channels by phospholipase C‐dependent mechanisms. The Journal Of Physiology 2001, 530: 1-19. PMID: 11136854, PMCID: PMC2278390, DOI: 10.1111/j.1469-7793.2001.0001m.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBaculoviridaeCalciumCalmodulin-Binding ProteinsCell LineCHO CellsCricetinaeDrosophilaDrosophila ProteinsFluorescent DyesFura-2Indicators and ReagentsMembrane PotentialsMembrane ProteinsOocytesPatch-Clamp TechniquesPhosphatidylinositol 4,5-DiphosphateSpodopteraTransient Receptor Potential ChannelsType C PhospholipasesXenopusConceptsPhospholipase CPhospholipase DDrosophila TRPL channelsTRPL channel activitySf9 insect cellsBacterial PI-PLCsPLC-dependent mechanismChannel activityFura-2 assayReceptor stimulationHydrolysis of PIP2Generation of diacylglycerolPoly-unsaturated fatty acidsTRPL channelsReceptor-mediated activationAddition of phosphatidylinositolInsect cellsExogenous applicationPI-PLCTransient receptor potential-like channelPC-PLCPIP2Spontaneous channel activityTRPLDiacylglycerol
1999
Stimulation of Drosophila TrpL by capacitative Ca2+ entry.
Estacion M, Sinkins W, Schilling W. Stimulation of Drosophila TrpL by capacitative Ca2+ entry. Biochemical Journal 1999, 341 ( Pt 1): 41-9. PMID: 10377243, PMCID: PMC1220328, DOI: 10.1042/0264-6021:3410041.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBariumBiological TransportCalciumCalcium-Transporting ATPasesCalmodulinCalmodulin-Binding ProteinsCations, DivalentDrosophilaDrosophila ProteinsEndoplasmic ReticulumHumansIon Channel GatingIon ChannelsLanthanumMembrane ProteinsPatch-Clamp TechniquesRecombinant Fusion ProteinsSpodopteraStrontiumThapsigarginTransient Receptor Potential ChannelsConceptsCapacitative Ca2Internal Ca2Receptor-activated channelsCell-attached patch recordingsTRP-like proteinsNon-selective cation channelsCytosolic free Ca2CBS-2Fura-2Cation entryPatch recordingsHuman TRPC1Single-channel activityDrosophila TRPLTRPL activityFree Ca2Dependent mechanismCation influxGel overlay experimentsCation channelsPhotoreceptor cellsChannel activityPhospholipase CTRPC1TRPL channel activity