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
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
2000
Permeation and gating residues in serotonin transporter
Chen J, Rudnick G. Permeation and gating residues in serotonin transporter. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 1044-1049. PMID: 10655481, PMCID: PMC15515, DOI: 10.1073/pnas.97.3.1044.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAmino Acid SubstitutionCarrier ProteinsChloridesCocaineHumansHydrogenIon Channel GatingIon TransportIsoleucineMembrane GlycoproteinsMembrane Transport ProteinsMesylatesMutagenesis, Site-DirectedNerve Tissue ProteinsNorepinephrine Plasma Membrane Transport ProteinsOxidation-ReductionPotassiumProtein BindingProtein ConformationProtein Structure, TertiaryRecombinant Fusion ProteinsReducing AgentsSerotoninSerotonin Plasma Membrane Transport ProteinsSodiumSulfhydryl CompoundsSymportersConceptsSubstrate permeation pathway
1996
Ion Coupling Stoichiometry for the Norepinephrine Transporter in Membrane Vesicles from Stably Transfected Cells (∗)
Gu H, Wall S, Rudnick G. Ion Coupling Stoichiometry for the Norepinephrine Transporter in Membrane Vesicles from Stably Transfected Cells (∗). Journal Of Biological Chemistry 1996, 271: 6911-6916. PMID: 8636118, DOI: 10.1074/jbc.271.12.6911.Peer-Reviewed Original ResearchConceptsMembrane vesiclesTransmembrane ion gradientsLLC-PK1 cellsMajor substrateTransport substratesTransfected CellsStably Transfected CellsIon gradientsCoupling stoichiometryNet positive chargeDA accumulationVesiclesSubstrate moleculesTransportersNorepinephrine transporterAccumulationCellsGamma-aminobutyric acidCotransportDAGradientStoichiometrySubstrateAbsenceTransport processes
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
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
1985
Serotonin Transport by Platelet Plasma and Granule Membranes
RUDNICK G, HUMPHREYS C, DEAN G. Serotonin Transport by Platelet Plasma and Granule Membranes. Annals Of The New York Academy Of Sciences 1985, 456: 277-278. PMID: 2418730, DOI: 10.1111/j.1749-6632.1985.tb14876.x.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsEffects of monovalent cations on Semliki Forest virus entry into BHK-21 cells.
Helenius A, Kielian M, Wellsteed J, Mellman I, Rudnick G. Effects of monovalent cations on Semliki Forest virus entry into BHK-21 cells. Journal Of Biological Chemistry 1985, 260: 5691-5697. PMID: 3988769, DOI: 10.1016/s0021-9258(18)89078-0.Peer-Reviewed Original ResearchConceptsSemliki Forest virusEndosome membraneViral envelopeBaby hamster kidney cellsMammalian cellsEndosomal membranesLow endosomalBHK-21 cellsHamster kidney cellsVirus endocytosisIntact cellsConformational changesEndosomesPrelysosomal endosomesViral spike glycoproteinVirus fusionKidney cellsAcidic endosomal pHViral RNAVoltage-sensitive probeEndocytosisVirus entryEndosomal pHCellsSpike glycoprotein
1983
Hydrogen ion cotransport by the renal brush border glutamate transporter.
Nelson P, Dean G, Aronson P, Rudnick G. Hydrogen ion cotransport by the renal brush border glutamate transporter. Biochemistry 1983, 22: 5459-63. PMID: 6140027, DOI: 10.1021/bi00292a030.Peer-Reviewed Original Research
1982
Coupling of transmembrane proton gradients to platelet serotonin transport.
Keyes S, Rudnick G. Coupling of transmembrane proton gradients to platelet serotonin transport. Journal Of Biological Chemistry 1982, 257: 1172-1176. PMID: 7056713, DOI: 10.1016/s0021-9258(19)68170-6.Peer-Reviewed Original ResearchConceptsPlasma membrane vesiclesSerotonin transportTransmembrane proton gradientPlatelet plasma membraneTransmembrane ion gradientsApparent competitionPlasma membraneMembrane vesiclesProton gradientIon gradientsSerotonin accumulationSole driving forceVesiclesAccumulationSerotonin transporterPH differencePhysiological pHTransportersTransportPH stimulationMembraneGradient
1978
Reconstitution of 5-hydroxytryptamine transport from cholate-disrupted platelet plasma membrane vesicles.
Rudnick G, Nelson P. Reconstitution of 5-hydroxytryptamine transport from cholate-disrupted platelet plasma membrane vesicles. Biochemistry 1978, 17: 5300-3. PMID: 728400, DOI: 10.1021/bi00617a033.Peer-Reviewed Original ResearchConceptsPlatelet plasma membrane vesiclesPlasma membrane vesiclesMembrane vesiclesTransport activityNative membrane vesiclesHigh molecular weight aggregatesInhibitor sensitivityVesicular structuresVesiclesIntact plateletsWeight aggregatesIonic requirementsSoybean phospholipidsProteoliposomesTransportersActivityPhospholipidsReconstitutionPlatelet 5-hydroxytryptamine transport, an electroneutral mechanism coupled to potassium.
Rudnick G, Nelson P. Platelet 5-hydroxytryptamine transport, an electroneutral mechanism coupled to potassium. Biochemistry 1978, 17: 4739-42. PMID: 728383, DOI: 10.1021/bi00615a021.Peer-Reviewed Original ResearchConceptsPlasma membrane vesiclesLipophilic cation triphenylmethylphosphoniumMembrane potentialMembrane vesiclesElectroneutral mechanismVesicle membraneIon effluxPorcine blood plateletsAbsence of valinomycinAddition of valinomycinPotassium gradientBlood plateletsValinomycinElectrogenic mechanismMembraneNet influxMechanismDinitrophenolVesiclesTransportLittle effectInfluxTriphenylmethylphosphoniumAbsenceEfflux