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
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 Vesicles
2007
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*
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