2016
Control of serotonin transporter phosphorylation by conformational state
Zhang YW, Turk BE, Rudnick G. Control of serotonin transporter phosphorylation by conformational state. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: e2776-e2783. PMID: 27140629, PMCID: PMC4878475, DOI: 10.1073/pnas.1603282113.Peer-Reviewed Original ResearchConceptsTransmembrane helix 5Cytoplasmic permeation pathwaysOutward open conformationIntact rat basophilic leukemia cellsCGMP-dependent phosphorylationInhibition of phosphorylationTM5 helicesTransporter phosphorylationSERT regulationOutward openingCysteine residuesHelix 5Open conformationCytoplasmic endHuman SERTPhosphorylationPermeation pathwayConformational statesHeLa cellsRat basophilic leukemia cellsBasophilic leukemia cellsSERT activityExocytotic releaseLeukemia cellsMutations
2009
Ligand Effects on Cross-linking Support a Conformational Mechanism for Serotonin Transport*
Tao Z, Zhang YW, Agyiri A, Rudnick G. Ligand Effects on Cross-linking Support a Conformational Mechanism for Serotonin Transport*. Journal Of Biological Chemistry 2009, 284: 33807-33814. PMID: 19837674, PMCID: PMC2797150, DOI: 10.1074/jbc.m109.071977.Peer-Reviewed Original ResearchConceptsN-terminal cyanogen bromide fragmentGamma-aminobutyric acid transporterCyanogen bromide fragmentsTransmembrane 1Cysteine residuesMutagenesis strategyAcid transportersConformational mechanismSerotonin transportCysteineCorresponding positionDisulfide CrossTransportersSynaptic cleftResiduesSame molecule
2000
Functional Role of Critical Stripe Residues in Transmembrane Span 7 of the Serotonin Transporter EFFECTS OF Na+, Li+, AND METHANETHIOSULFONATE REAGENTS*
Kamdar G, Penado K, Rudnick G, Stephan M. Functional Role of Critical Stripe Residues in Transmembrane Span 7 of the Serotonin Transporter EFFECTS OF Na+, Li+, AND METHANETHIOSULFONATE REAGENTS*. Journal Of Biological Chemistry 2000, 276: 4038-4045. PMID: 11058600, DOI: 10.1074/jbc.m008483200.Peer-Reviewed Original ResearchConceptsCys-109Methanethiosulfonate reagentsWater-filled poresNative cysteine residuesCysteine-containing mutantsExtracellular loop 1Close-contact regionThree-dimensional structureCysteine residuesTranslocation mechanismControl mutantsAlpha-helixMTSEA-biotinResidue positionsCysteine substitutionsLoop 1Conformational changesMTS reagentsFunctional roleMutantsIon bindingResiduesTransportersIon dependenceSerotonin transporter
1997
External 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