2007
Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1
Castagna M, Soragna A, Mari S, Santacroce M, Betté S, Mandela P, Rudnick G, Peres A, Sacchi V. Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1. American Journal Of Physiology - Cell Physiology 2007, 293: c1286-c1295. PMID: 17626242, DOI: 10.1152/ajpcell.00190.2007.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAmino Acid Transport Systems, NeutralAnimalsAspartic AcidBinding SitesBiological TransportCross-Linking ReagentsCysteineDithiothreitolFemaleInsect ProteinsKineticsLepidopteraLysineModels, MolecularMolecular Sequence DataOocytesPhenanthrolinesPotassiumProtein Structure, TertiarySequence Homology, Amino AcidSodiumTryptophanXenopus laevisConceptsSingle cysteine mutantsNeutral amino acid transporterSite-directed mutagenesisAmino acid transportersTransport-associated currentNSS transportersDouble mutantXenopus laevis oocytesCysteine mutantsWild typeDependent transportLysine 102MutantsSuper familyAcid transportersPermeation pathwayAmino acidsDisulfide bondsLaevis oocytesFunctional evidenceAsp338Leucine uptakeKAAT1Spatial organizationResidues
1999
The Role of External Loop Regions in Serotonin Transport LOOP SCANNING MUTAGENESIS OF THE SEROTONIN TRANSPORTER EXTERNAL DOMAIN*
Smicun Y, Campbell S, Chen M, Gu H, Rudnick G. The Role of External Loop Regions in Serotonin Transport LOOP SCANNING MUTAGENESIS OF THE SEROTONIN TRANSPORTER EXTERNAL DOMAIN*. Journal Of Biological Chemistry 1999, 274: 36058-36064. PMID: 10593887, DOI: 10.1074/jbc.274.51.36058.Peer-Reviewed Original ResearchConceptsChimeric transportersWild type SERTExternal loop 4High affinity cocaine analogSubsequent conformational changesExternal loop regionsTransmembrane segmentsInitial binding stepScanning mutagenesisWild typeExternal loopLigand bindingSerotonin transporterMutantsConformational changesLoop 4Loop regionConformational flexibilityTransportersCorresponding sequenceBinding stepExternal domainNorepinephrine transporterActivity 5NET substrate
1998
Critical Amino Acid Residues in Transmembrane Span 7 of the Serotonin Transporter Identified by Random Mutagenesis*
Penado K, Rudnick G, Stephan M. Critical Amino Acid Residues in Transmembrane Span 7 of the Serotonin Transporter Identified by Random Mutagenesis*. Journal Of Biological Chemistry 1998, 273: 28098-28106. PMID: 9774428, DOI: 10.1074/jbc.273.43.28098.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsMembrane GlycoproteinsMembrane Transport ProteinsModels, MolecularMolecular Sequence DataMutagenesisNerve Tissue ProteinsProtein ConformationRatsSerotoninSerotonin Plasma Membrane Transport ProteinsStructure-Activity RelationshipConceptsAmino acid residuesRandom mutagenesisAcid residuesTransport activityCritical amino acid residuesRat brain serotonin transporterCritical residuesTransport cycleWild typeNonconservative mutationsStructural predictionsTransporter functionLater stepsMutationsSerotonin transporterResiduesMutagenesisHydrophobic substitutionsTyr-385TransportersMutantsActivitySubstitutionNearby positions
1997
An Extracellular Loop Region of the Serotonin Transporter May Be Involved in the Translocation Mechanism †
Stephan M, Chen M, Penado K, Rudnick G. An Extracellular Loop Region of the Serotonin Transporter May Be Involved in the Translocation Mechanism †. Biochemistry 1997, 36: 1322-1328. PMID: 9063880, DOI: 10.1021/bi962150l.Peer-Reviewed Original ResearchConceptsLarge extracellular loopChimeric transportersWild typeWild type SERTExtracellular loopCocaine analog 2beta-carbomethoxy-3betaCell surface biotinylationWild-type levelsSubstrate translocationExtracellular loop regionSurface biotinylationTranslocation mechanismSerotonin transporterHomologous familyType levelsConformational changesLoop regionRestriction sitesTransportersPoor expressionSubstituted regionsSynaptic cleftDrug bindingSame specificityHigh affinityExternal Cysteine Residues in the Serotonin Transporter †
Chen J, Liu-Chen S, Rudnick G. External Cysteine Residues in the Serotonin Transporter †. Biochemistry 1997, 36: 1479-1486. PMID: 9063896, DOI: 10.1021/bi962256g.Peer-Reviewed Original ResearchConceptsTransport activityMTS reagentsCysteine residuesWild typeWild-type transporterSecond external loopTransient expression systemSurface expressionRat serotonin transporterExternal cysteine residuesHydropathy analysisMutant transportersType transporterDouble mutantExpression systemMethanethiosulfonate reagentsLigand bindingSerotonin transporterMutantsExtracellular loopHeLa cellsDisulfide bondsPartial activityTransportersSerine