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