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