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
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
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
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