2016
Na+ coordination at the Na2 site of the Na+/I− symporter
Ferrandino G, Nicola JP, Sánchez YE, Echeverria I, Liu Y, Amzel LM, Carrasco N. Na+ coordination at the Na2 site of the Na+/I− symporter. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: e5379-e5388. PMID: 27562170, PMCID: PMC5027462, DOI: 10.1073/pnas.1607231113.Peer-Reviewed Original ResearchConceptsNa2 siteActive I(-) transportThyroid hormone biosynthesisSodium/iodide symporterSLC5 familyGreat medical relevanceSame foldPlasma membraneHormone biosynthesisDependent transportersSimilar functionsMedical relevanceTransportersMechanistic insightsWhole cellsBinding sitesResiduesSymporterI- transportS353Side chainsT354SitesBiosynthesisIons bind
2014
Physiological sodium concentrations enhance the iodide affinity of the Na+/I− symporter
Nicola JP, Carrasco N, Mario Amzel L. Physiological sodium concentrations enhance the iodide affinity of the Na+/I− symporter. Nature Communications 2014, 5: 3948. PMID: 24888603, PMCID: PMC4248369, DOI: 10.1038/ncomms4948.Peer-Reviewed Original Research
2013
Asn441 plays a key role in folding and function of the Na+/I– symporter (NIS)
Li W, Nicola JP, Amzel LM, Carrasco N. Asn441 plays a key role in folding and function of the Na+/I– symporter (NIS). The FASEB Journal 2013, 27: 3229-3238. PMID: 23650190, PMCID: PMC3714583, DOI: 10.1096/fj.13-229138.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAsparagineBinding SitesBiological TransportCell LineCell MembraneChlorocebus aethiopsCOS CellsHumansImmunoblottingIodineMicroscopy, ConfocalModels, MolecularMolecular Sequence DataMutationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidSymportersTransport VesiclesThe iodide-transport-defect-causing mutation R124H: a δ-amino group at position 124 is critical for maturation and trafficking of the Na+/I− symporter
Paroder V, Nicola JP, Ginter CS, Carrasco N. The iodide-transport-defect-causing mutation R124H: a δ-amino group at position 124 is critical for maturation and trafficking of the Na+/I− symporter. Journal Of Cell Science 2013, 126: 3305-3313. PMID: 23690546, PMCID: PMC3730242, DOI: 10.1242/jcs.120246.Peer-Reviewed Original ResearchConceptsPlasma membranePlasma membrane traffickingPosition 124Key structural roleCOS-7 cellsSecond intracellular loopAmino acid substitutionsMembrane traffickingTransporter maturationNIS mutantsIntracellular loopEndoplasmic reticulumStructural roleMembrane vesiclesThyroid hormone T3I- transportAcid substitutionsHomology modelCell surfaceTransport defectProtein markersLocal foldingSymporterMutantsVibrio parahaemolyticus
2011
Mechanism of anion selectivity and stoichiometry of the Na+/I- symporter (NIS)
Paroder-Belenitsky M, Maestas MJ, Dohán O, Nicola JP, Reyna-Neyra A, Follenzi A, Dadachova E, Eskandari S, Amzel LM, Carrasco N. Mechanism of anion selectivity and stoichiometry of the Na+/I- symporter (NIS). Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 17933-17938. PMID: 22011571, PMCID: PMC3207644, DOI: 10.1073/pnas.1108278108.Peer-Reviewed Original Research
2007
The Na+/I− symporter (NIS) mediates electroneutral active transport of the environmental pollutant perchlorate
Dohán O, Portulano C, Basquin C, Reyna-Neyra A, Amzel LM, Carrasco N. The Na+/I− symporter (NIS) mediates electroneutral active transport of the environmental pollutant perchlorate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 20250-20255. PMID: 18077370, PMCID: PMC2154417, DOI: 10.1073/pnas.0707207104.Peer-Reviewed Original ResearchConceptsI- uptakeExposure of newbornsDifferent stoichiometriesIodine-containing thyroid hormonesPublic health impactStoichiometryMaternal milkLactating breastPerchlorateGreater health risksThyroid hormonesEnvironmental pollutant perchlorateDifferent substratesCNS developmentSuch exposureU.S. populationProper CNS developmentCompetitive inhibitorHealth impactsNewbornsKey plasma membrane proteinThyroidBreastHealth risksAnionsAmino Acid Residues in Transmembrane Segment IX of the Na+/I– Symporter Play a Role in Its Na+ Dependence and Are Critical for Transport Activity*
De la Vieja A, Reed MD, Ginter CS, Carrasco N. Amino Acid Residues in Transmembrane Segment IX of the Na+/I– Symporter Play a Role in Its Na+ Dependence and Are Critical for Transport Activity*. Journal Of Biological Chemistry 2007, 282: 25290-25298. PMID: 17606623, DOI: 10.1074/jbc.m700147200.Peer-Reviewed Original ResearchConceptsMembrane/cytosol interfaceActive I(-) transportAmino acid residuesPlasma membrane glycoproteinsBinding/translocationProtein familySegment IXNIS mutationPosition 354Asp-369NIS functionAcid residuesTransport activityMembrane glycoproteinsAmino acidsFunctional significanceResiduesSymporterI- transportKey roleSide chainsTranslocationTransportersThrHelix
1999
Escape from the acute Wolff-Chaikoff effect is associated with a decrease in thyroid sodium/iodide symporter messenger ribonucleic acid and protein.
Eng P, Cardona G, Fang S, Previti M, Alex S, Carrasco N, Chin W, Braverman L. Escape from the acute Wolff-Chaikoff effect is associated with a decrease in thyroid sodium/iodide symporter messenger ribonucleic acid and protein. Endocrinology 1999, 140: 3404-10. PMID: 10433193, DOI: 10.1210/endo.140.8.6893.Peer-Reviewed Original ResearchConceptsAcute Wolff-Chaikoff effectThyroid peroxidase mRNANIS mRNAIodide administrationWolff-Chaikoff effectThyroid peroxidaseIodide transportTSH receptorNIS proteinIodide ingestionIntrathyroidal iodine contentIodine-induced hypothyroidismSerum TSH levelsOrganification of iodideAcute experimentsIodide-induced changesMessenger ribonucleic acidPlasma iodide levelsTSH levelsHashimoto's thyroiditisChronic experimentsSerum T4Plasma iodide concentrationsSodium/iodide symporterHormone measurements