2024
Identification of the potassium-binding site in serotonin transporter
Hellsberg E, Boytsov D, Chen Q, Niello M, Freissmuth M, Rudnick G, Zhang Y, Sandtner W, Forrest L. Identification of the potassium-binding site in serotonin transporter. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2319384121. PMID: 38652746, PMCID: PMC11067047, DOI: 10.1073/pnas.2319384121.Peer-Reviewed Original ResearchConceptsSerotonin transporterSite-directed mutagenesis of residuesMutagenesis of residuesSite-directed mutagenesisHeterologous expression systemStudy of vesiclesNa2 siteClearance of serotoninPatch-clamp recordingsExpression systemBinding residuesSequential bindingMolecular dynamics simulationsBinding sitesPotassium binding siteSubstrate accumulationClamp recordingsVesiclesResiduesTurnover rateBindingStructural studiesChemical gradientsBinding configurationsSynaptic cleft
2018
Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT
Zhang YW, Tavoulari S, Sinning S, Aleksandrova AA, Forrest LR, Rudnick G. Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: e8854-e8862. PMID: 30181291, PMCID: PMC6156673, DOI: 10.1073/pnas.1716870115.Peer-Reviewed Original ResearchConceptsTransporter domainConformational changesOpen stateSodium symporter familyIon-substrate couplingTransmembrane ion gradientsSymporter familyNSS transportersSubstrate bindingLeuTIntracellular substratesCysteine accessibilitySubstrate transportAccessibility of substrateTyrosine residuesConformational responseNa2 siteUncoupled movementIon gradientsExtracellular pathwaysMechanistic componentsTransportersProteinTransport of ionsBinding
1993
Non-neurotoxic amphetamine derivatives release serotonin through serotonin transporters.
Rudnick G, Wall S. Non-neurotoxic amphetamine derivatives release serotonin through serotonin transporters. Molecular Pharmacology 1993, 43: 271-6. PMID: 8429828.Peer-Reviewed Original ResearchMeSH KeywordsAmphetaminesBlood PlateletsCarrier ProteinsCell MembraneChromaffin GranulesHumansImipramineIn Vitro TechniquesIndansMembrane GlycoproteinsMembrane Transport ProteinsMethamphetamineModels, BiologicalNerve EndingsNerve Tissue ProteinsRadioligand AssaySerotoninSerotonin Plasma Membrane Transport ProteinsConceptsChromaffin granule membrane vesiclesPlasma membrane vesiclesMembrane vesiclesPlatelet plasma membrane vesiclesPlasma membrane transportersSerotonin transportBiogenic amine transportersMembrane transportersAmine transportersTransportersVesiclesDopamine transporterSerotonin transporterModel systemHalf-maximal concentrationNerve terminalsTransmembraneCocaine analogBindingSimilar concentrationsHigh concentrationsCellsTransport
1992
The 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 actionMechanismBindingMembrane
1990
Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter.
Rudnick G, Steiner-Mordoch S, Fishkes H, Stern-Bach Y, Schuldiner S. Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter. Biochemistry 1990, 29: 603-8. PMID: 2140052, DOI: 10.1021/bi00455a002.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmmonium SulfateBinding SitesBiogenic AminesCarbonyl Cyanide m-Chlorophenyl HydrazoneCarrier ProteinsChloridesChromaffin GranulesChromaffin SystemDetergentsElectrochemistryHydrogen-Ion ConcentrationIonophoresKineticsLigandsMembrane PotentialsReserpineThermodynamicsThiocyanatesTime FactorsUreaConceptsBiogenic amine transportersReserpine bindingChromaffin granule membrane vesiclesAmine transportersAmine transportMembrane vesiclesDead-end complexIon translocationTransportersSubstrate moleculesBindingM ureaDelta pHTranslocationTriton XSodium dodecyl sulfateNeutral substrate moleculesTransmembraneHigh-affinity site
1979
Mechanism of imipramine inhibition of platelet 5-hydroxytryptamine transport.
Talvenheimo J, Nelson P, Rudnick G. Mechanism of imipramine inhibition of platelet 5-hydroxytryptamine transport. Journal Of Biological Chemistry 1979, 254: 4631-4635. PMID: 438209, DOI: 10.1016/s0021-9258(17)30057-1.Peer-Reviewed Original Research
1976
Equilibrium between two forms of the lac carrier protein in energized and nonenergized membrane vesicles from Escherichia coli.
Rudnick G, Schuldiner S, Kaback H. Equilibrium between two forms of the lac carrier protein in energized and nonenergized membrane vesicles from Escherichia coli. Biochemistry 1976, 15: 5126-31. PMID: 791364, DOI: 10.1021/bi00668a028.Peer-Reviewed Original ResearchConceptsLac carrier proteinMembrane vesiclesCarrier proteinY gene productEscherichia coli ML 308P-nitrophenyl alphaD-lactateMembrane proteinsGene productsML 308Cryptic formVesicle membraneLactose transportElectrochemical gradientEscherichia coliEnergy couplingProteinVesiclesCarbonyl cyanideSimilar affinityCompetitive inhibitorHigh affinity formMembraneBindingFlow dialysisMechanism of β-galactoside transport in Escherichia coli membrane vesicles
Schuldiner S, Rudnick G, Weil R, Kaback H. Mechanism of β-galactoside transport in Escherichia coli membrane vesicles. Trends In Biochemical Sciences 1976, 1: 41-45. DOI: 10.1016/s0968-0004(76)80181-8.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
1975
ACTIVE TRANSPORT IN ISOLATED BACTERIAL MEMBRANE VESICLES: BINDING OF β‐GALACTOSIDES TO THE LAC CARRIER PROTEIN
Kaback H, Rudnick G, Schuldiner S, Short S. ACTIVE TRANSPORT IN ISOLATED BACTERIAL MEMBRANE VESICLES: BINDING OF β‐GALACTOSIDES TO THE LAC CARRIER PROTEIN. Annals Of The New York Academy Of Sciences 1975, 264: 350-357. PMID: 769642, DOI: 10.1111/j.1749-6632.1975.tb31495.x.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements