2019
Serotonin transport in the 21st century
Rudnick G, Sandtner W. Serotonin transport in the 21st century. The Journal Of General Physiology 2019, 151: 1248-1264. PMID: 31570504, PMCID: PMC6829555, DOI: 10.1085/jgp.201812066.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportHumansSerotoninSerotonin Plasma Membrane Transport ProteinsSynaptic Transmission
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
2013
How do transporters couple solute movements?
Rudnick G. How do transporters couple solute movements? Molecular Membrane Biology 2013, 30: 355-359. PMID: 24147977, PMCID: PMC4077868, DOI: 10.3109/09687688.2013.842658.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsBinding SitesBiological TransportCarrier ProteinsIon TransportLigandsMembrane Transport ProteinsModels, MolecularProtein Conformation
2010
Reconstructing a Chloride-binding Site in a Bacterial Neurotransmitter Transporter Homologue*
Tavoulari S, Rizwan AN, Forrest LR, Rudnick G. Reconstructing a Chloride-binding Site in a Bacterial Neurotransmitter Transporter Homologue*. Journal Of Biological Chemistry 2010, 286: 2834-2842. PMID: 21115480, PMCID: PMC3024779, DOI: 10.1074/jbc.m110.186064.Peer-Reviewed Original ResearchConceptsChloride-binding siteConformational changesAdjacent binding sitesSingle point mutationProkaryotic homologuesSubstrate translocationIon-binding sitesTransporter homologueTransport proteinsNeurotransmitter transportersNeurotransmitter transportPoint mutationsBinding sitesHomologuesProteinMutationsCl(-) bindsDirect evidenceTherapeutic drugsSitesDependent formTranslocationTransportersBindsResidues
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
2008
Involvement of serotonin transporter extracellular loop 1 in serotonin binding and transport
Mao Y, Mao Y, Mathewson L, Mao Y, Mathewson L, Gesmonde J, Sato Y, Mao Y, Mathewson L, Gesmonde J, Sato Y, Holy M, Sitte H, Rudnick G. Involvement of serotonin transporter extracellular loop 1 in serotonin binding and transport. Molecular Membrane Biology 2008, 25: 115-127. PMID: 18307099, PMCID: PMC4510095, DOI: 10.1080/09687680701633257.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCell MembraneHeLa CellsHumansIndicators and ReagentsKineticsLigandsMesylatesMolecular Sequence DataMutant ProteinsProtein Structure, TertiaryRatsSequence DeletionSerotoninSerotonin Plasma Membrane Transport ProteinsStructure-Activity Relationship
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[16] Ion-coupled neurotransmitter transport: Thermodynamic vs. kinetic determinations of stoichiometry
Rudnick G. [16] Ion-coupled neurotransmitter transport: Thermodynamic vs. kinetic determinations of stoichiometry. Methods In Enzymology 1998, 296: 233-247. PMID: 9779452, DOI: 10.1016/s0076-6879(98)96018-9.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsNumber of ionsKinetic determinationMolecular machinesCharge movesIonsLipid bilayersNeurotransmitter moleculesMoleculesInput of energySteady-state distributionLow concentrationsChargeElectrical potentialMembraneIon gradientsStoichiometryHigh concentrationsUltimate concentrationNaConcentrationEnergyBilayersNeurotransmitter transportersNumber of NaNeurotransmitter transport
1996
Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*
Gu H, Ahn J, Caplan M, Blakely R, Levey A, Rudnick G. Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*. Journal Of Biological Chemistry 1996, 271: 18100-18106. PMID: 8663573, DOI: 10.1074/jbc.271.30.18100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiogenic AminesBiological TransportCarrier ProteinsCell CompartmentationCell MembraneCell PolarityCells, CulturedDogsDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansImmunohistochemistryMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsRatsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSymportersConceptsMadin-Darby canine kidneyMDCK cellsLLC-PK1 cellsNeurotransmitter transportersCell surface biotinylationConfocal immunofluorescence microscopyBasolateral membraneCell-specific mechanismsEpithelial cellsBiogenic amine transportersMembrane proteinsSurface biotinylationCDNA encodingHuman DA transporterAmine transportersImmunofluorescence microscopyBiotinylating reagentTransportersPermeable filter supportsApical surfaceImmunocytochemistry resultsBasolateral mediumSurface expressionApical sideDA transporter
1995
Biogenic amine flux mediated by cloned transporters stably expressed in cultured cell lines: amphetamine specificity for inhibition and efflux.
Wall S, Gu H, Rudnick G. Biogenic amine flux mediated by cloned transporters stably expressed in cultured cell lines: amphetamine specificity for inhibition and efflux. Molecular Pharmacology 1995, 47: 544-50. PMID: 7700252.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-4-phenylpyridiniumAmphetaminesBiogenic MonoaminesBiological TransportCarrier ProteinsCell MembraneCells, CulturedCloning, MolecularCocaineDNA, ComplementaryDopamineDopamine Plasma Membrane Transport ProteinsHumansMazindolMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNeurotransmitter Uptake InhibitorsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsStimulation, ChemicalSubstrate SpecificitySymportersTransfectionConceptsBiogenic amine transportersCell linesAmine transportersRat serotonin transporterCultured cell linesInhibitor of transportRat dopamine transporterHuman norepinephrine transporterPlasma membraneLLC-PK1 cellsSubstrate effluxSubstrate influxDopamine transporterNorepinephrine transporterAmphetamine derivativesTransportersSerotonin transporterEffluxDistinct patternsP-chloroamphetamineAmine substratesCellsInhibited transportCDNAInhibitors
1994
Stable expression of biogenic amine transporters reveals differences in inhibitor sensitivity, kinetics, and ion dependence.
Gu H, Wall S, Rudnick G. Stable expression of biogenic amine transporters reveals differences in inhibitor sensitivity, kinetics, and ion dependence. Journal Of Biological Chemistry 1994, 269: 7124-7130. PMID: 8125921, DOI: 10.1016/s0021-9258(17)37256-3.Peer-Reviewed Original ResearchAnimalsBinding SitesBiogenic AminesBiological TransportCarrier ProteinsCell LineDopamine Plasma Membrane Transport ProteinsHumansKineticsMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrine Plasma Membrane Transport ProteinsRatsRecombinant ProteinsSerotonin Plasma Membrane Transport ProteinsSymportersTransfection
1992
p-Chloroamphetamine induces serotonin release through serotonin transporters.
Rudnick G, Wall S. p-Chloroamphetamine induces serotonin release through serotonin transporters. Biochemistry 1992, 31: 6710-8. PMID: 1322169, DOI: 10.1021/bi00144a010.Peer-Reviewed Original ResearchMeSH KeywordsBinding, CompetitiveBiological TransportBlood PlateletsCarrier ProteinsCell MembraneChloridesHumansHydrogen-Ion ConcentrationImipramineKineticsLithiumLithium ChlorideMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsP-ChloroamphetamineRadioisotope Dilution TechniqueSerotoninSerotonin Plasma Membrane Transport ProteinsTritiumConceptsPlasma membrane vesiclesMembrane vesiclesChromaffin granule membrane vesiclesVesicular amine transporterATP hydrolysisBovine adrenal chromaffin granulesSerotonin transporterAdrenal chromaffin granulesPrevents accumulationAmine transportersPresence of Mg2TransportersVesiclesChromaffin granulesModel systemDelta pHHuman plateletsATPEffluxManner characteristicAccumulationTransmembraneNaCl gradientPCA's abilityP-chloroamphetamineThe molecular mechanism of "ecstasy" [3,4-methylenedioxy-methamphetamine (MDMA)]: serotonin transporters are targets for MDMA-induced serotonin release.
Rudnick G, Wall S. The molecular mechanism of "ecstasy" [3,4-methylenedioxy-methamphetamine (MDMA)]: serotonin transporters are targets for MDMA-induced serotonin release. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 1817-1821. PMID: 1347426, PMCID: PMC48544, DOI: 10.1073/pnas.89.5.1817.Peer-Reviewed Original ResearchConceptsPlasma membrane vesiclesMembrane vesiclesAmine transportersVesicular amine transporterBiogenic amine transportersSecretory vesiclesPlasma membraneATP hydrolysisMolecular mechanismsBovine adrenal chromaffin granulesSerotonin transporterAdrenal chromaffin granulesTransportersDirect interactionVesiclesChromaffin granulesHuman plateletsManner characteristicEffluxTransmembraneATPMDMA actionMechanismBindingMembraneExpression of a cloned gamma-aminobutyric acid transporter in mammalian cells.
Keynan S, Suh Y, Kanner B, Rudnick G. Expression of a cloned gamma-aminobutyric acid transporter in mammalian cells. Biochemistry 1992, 31: 1974-9. PMID: 1536839, DOI: 10.1021/bi00122a011.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCarrier ProteinsChloridesCloning, MolecularDNAGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidGene ExpressionGenetic VectorsHeLa CellsHumansKineticsL CellsMembrane ProteinsMembrane Transport ProteinsMiceNerve Tissue ProteinsOrganic Anion TransportersPlasmidsPrecipitin TestsRatsSodiumTransfectionTunicamycinXenopusConceptsMammalian cellsGABA transportMouse Ltk- cellsT7 RNA polymerasePlasma membrane vesiclesL cellsApparent molecular massGABA transporterSynaptic plasma membrane vesiclesGamma-aminobutyric acid transporterPresence of tunicamycinEukaryotic expression vectorRNA polymeraseTransient expressionExpression vectorAcid transportersMembrane vesiclesStable expressionLtk- cellsFunctional expressionGAT-1Molecular massHeLa cellsTransportersTransfectionPlatelet serotonin transporter
Rudnick G, Humphreys C. Platelet serotonin transporter. Methods In Enzymology 1992, 215: 213-224. PMID: 1435323, DOI: 10.1016/0076-6879(92)15065-k.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsAdenosine TriphosphateAnimalsBiological TransportBlood PlateletsCarrier ProteinsCell FractionationCell MembraneCell SeparationCentrifugationHumansImipramineIndicators and ReagentsMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsRadioligand AssaySerotoninSerotonin Plasma Membrane Transport ProteinsSwineTritium
1991
Binding of the cocaine analog 2 beta-[3H] carboxymethoxy-3 beta-(4-fluorophenyl)tropane to the serotonin transporter.
Rudnick G, Wall S. Binding of the cocaine analog 2 beta-[3H] carboxymethoxy-3 beta-(4-fluorophenyl)tropane to the serotonin transporter. Molecular Pharmacology 1991, 40: 421-6. PMID: 1896028.Peer-Reviewed Original Research
1989
2-Iodoimipramine, a novel ligand for the serotonin transporter.
Humphreys C, Cassel D, Rudnick G. 2-Iodoimipramine, a novel ligand for the serotonin transporter. Molecular Pharmacology 1989, 36: 620-6. PMID: 2811859.Peer-Reviewed Original ResearchZwitterionic and Anionic Forms of a Serotonin Analog as Transport Substrates
Rudnick G, Kirk K, Fishkes H, Schuldiner S. Zwitterionic and Anionic Forms of a Serotonin Analog as Transport Substrates. Journal Of Biological Chemistry 1989, 264: 14865-14868. PMID: 2549040, DOI: 10.1016/s0021-9258(18)63781-0.Peer-Reviewed Original ResearchConceptsBiogenic amine transportersAmine transportersPlasma membrane serotonin transporterSubstrate translocationBovine chromaffin granulesTransport substratesHuman blood plateletsSerotonin transportChromaffin granulesTransportersBlood plateletsSerotonin transporterKmIdentical ratesTranslocationSubstrateTransport