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 ResearchConceptsTransmembrane 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 effluxHelixPathway
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
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 role