2015
A structural model for facultative anion channels in an oligomeric membrane protein: the yeast TRK (K+) system
Pardo JP, González-Andrade M, Allen K, Kuroda T, Slayman CL, Rivetta A. A structural model for facultative anion channels in an oligomeric membrane protein: the yeast TRK (K+) system. Pflügers Archiv - European Journal Of Physiology 2015, 467: 2447-2460. PMID: 26100673, DOI: 10.1007/s00424-015-1712-6.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceChloridesMolecular Sequence DataPotassiumPotassium ChannelsProtein Structure, TertiarySaccharomyces cerevisiae ProteinsYeastsConceptsTransmembrane helicesAnion channelTrk proteinNon-animal cellsOligomeric membrane proteinsAmphipathic transmembrane helicesLigand-gated anion channelsClass of proteinsTrk transportersRCK domainsBacterial membersRegulatory domainMembrane proteinsFungal proteinsTrk systemHydrophobic gatingPrimary sequenceMembrane voltageBiological membranesProteinCytoplasmic collarFunctional processesChloride effluxHelixPathwayYeast Fex1p Is a Constitutively Expressed Fluoride Channel with Functional Asymmetry of Its Two Homologous Domains*
Smith KD, Gordon PB, Rivetta A, Allen KE, Berbasova T, Slayman C, Strobel SA. Yeast Fex1p Is a Constitutively Expressed Fluoride Channel with Functional Asymmetry of Its Two Homologous Domains*. Journal Of Biological Chemistry 2015, 290: 19874-19887. PMID: 26055717, PMCID: PMC4528147, DOI: 10.1074/jbc.m115.651976.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell MembraneConserved SequenceDrug Resistance, FungalEscherichia coliFluoridesGene ExpressionGene Expression Regulation, FungalGenome, FungalIon TransportMembrane ProteinsMolecular Sequence DataMutationPatch-Clamp TechniquesPhosphorylationPhylogenyProtein FoldingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentStatic ElectricityConceptsC-terminal domainSaccharomyces cerevisiae functionsYeast plasma membraneN-terminal domainEffects of mutationsDuplicate proteinsYeast genomeCerevisiae functionsSequence conservationHelix domainLinker helixUbiquitous environmental toxinHomologous domainsImportant residuesFluoride channelsPlasma membraneParticular residuesBiological speciesSimilar mutationsIon channelsContinuous expressionProteinAntiparallel dimerMutationsResidues
2011
Anion currents in yeast K+ transporters (TRK) characterize a structural homologue of ligand-gated ion channels
Rivetta A, Kuroda T, Slayman C. Anion currents in yeast K+ transporters (TRK) characterize a structural homologue of ligand-gated ion channels. Pflügers Archiv - European Journal Of Physiology 2011, 462: 315-330. PMID: 21556692, PMCID: PMC3151154, DOI: 10.1007/s00424-011-0959-9.Peer-Reviewed Original Research
2009
Conservation and dispersion of sequence and function in fungal TRK potassium transporters: focus on Candida albicans
Miranda M, Bashi E, Vylkova S, Edgerton M, Slayman C, Rivetta A. Conservation and dispersion of sequence and function in fungal TRK potassium transporters: focus on Candida albicans. FEMS Yeast Research 2009, 9: 278-292. PMID: 19175416, DOI: 10.1111/j.1567-1364.2008.00471.x.Peer-Reviewed Original ResearchMeSH KeywordsCandida albicansCation Transport ProteinsChloridesConserved SequenceFungal ProteinsModels, BiologicalModels, MolecularPhylogenyPolymorphism, Single NucleotidePotassiumProtein ConformationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidConceptsPotassium transportersHuman pathogen Candida albicansTrk potassium transportersPathogen Candida albicansDetailed molecular investigationAnimal cellsSingle nucleotide polymorphismsDNA sequencesS. cerevisiaeComplete sequenceC. albicansTrk proteinSequence analysisCandida albicansInhibitor sensitivityFunctional comparisonNucleotide polymorphismsSelective drug actionMolecular investigationsAntimicrobial peptidesHomologuesPotential targetSecondary functionSalivary antimicrobial peptidesProtein
2005
Quantitative Modeling of Chloride Conductance in Yeast TRK Potassium Transporters
Rivetta A, Slayman C, Kuroda T. Quantitative Modeling of Chloride Conductance in Yeast TRK Potassium Transporters. Biophysical Journal 2005, 89: 2412-2426. PMID: 16040756, PMCID: PMC1366741, DOI: 10.1529/biophysj.105.066712.Peer-Reviewed Original ResearchMeSH KeywordsCation Transport ProteinsCell MembraneChlorineComputer SimulationElectric ConductivityHydrogen-Ion ConcentrationIon Channel GatingMembrane PotentialsModels, BiologicalModels, ChemicalSaccharomyces cerevisiae ProteinsConceptsTrk proteinTrk potassium transportersPotassium transportersYeast spheroplastsPlasma membraneCentral poreNegative membrane voltagesProteinActive accumulationChloride conductanceChloride currentsMembrane dielectricMembrane voltageSaccharomycesSpheroplastsFungiPlantsTransportersBacteriaConductanceMembrane slope conductanceHypothetical structural modelStructural modelMembraneSlope conductance
2004
The TRK1 Potassium Transporter Is the Critical Effector for Killing of Candida albicans by the Cationic Protein, Histatin 5*
Baev D, Rivetta A, Vylkova S, Sun JN, Zeng GF, Slayman CL, Edgerton M. The TRK1 Potassium Transporter Is the Critical Effector for Killing of Candida albicans by the Cationic Protein, Histatin 5*. Journal Of Biological Chemistry 2004, 279: 55060-55072. PMID: 15485849, DOI: 10.1074/jbc.m411031200.Peer-Reviewed Original ResearchMeSH Keywords4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic AcidAdenosine TriphosphateAllelesAnionsAntifungal AgentsAntimicrobial Cationic PeptidesBlotting, WesternCandida albicansCation Transport ProteinsCationsCell MembraneCell SeparationChloride ChannelsChloridesCytoplasmDNA PrimersDNA, ComplementaryDose-Response Relationship, DrugElectrophysiologyEscherichia coliFlow CytometryGene DeletionGenetic Complementation TestHistatinsHistidineModels, ChemicalModels, GeneticOligonucleotidesOpen Reading FramesPatch-Clamp TechniquesPlasmidsPotassiumProtease InhibitorsProtein BindingProtein Structure, TertiaryReverse Transcriptase Polymerase Chain ReactionRNARubidiumSaccharomyces cerevisiae ProteinsSalivary Proteins and PeptidesTime FactorsConceptsHst 5Hst 5 toxicityCritical effectorWild-type cellsTrk1 potassium transporterC. albicansPotassium transportersDiploid organismsOverexpression strainSingle copyCytoplasmic sequestrationPlasma membraneHistatin 5Essential pathwayPathogenic fungiCandida albicansAnion channel inhibitorsGenesTrk1pProteinATP lossChloride conductanceSmall moleculesEffectorsPossible roleChloride Channel Function in the Yeast TRK-Potassium Transporters
Kuroda T, Bihler H, Bashi E, Slayman CL, Rivetta A. Chloride Channel Function in the Yeast TRK-Potassium Transporters. The Journal Of Membrane Biology 2004, 198: 177-192. PMID: 15216418, DOI: 10.1007/s00232-004-0671-1.Peer-Reviewed Original Research