ArticleProceedings of the National Academy of Sciences of the United States of America2016
Na+ coordination at the Na2 site of the Na+/I- symporter.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Predicted T-Cell and B-Cell Epitopes of NIS: Where Do Sjögren's Syndrome and Hashimoto's Thyroiditis Converge?International journal of molecular sciences · 2025Article
- Functional characterization of novel compound heterozygous missenseFrontiers in endocrinology · 2024Article
- Sodium/Iodide Symporter Metastable Intermediates Provide Insights into Conformational Transition between Principal Thermodynamic States.The journal of physical chemistry. B · 2023Article
- Targeted Next-Generation Sequencing of Congenital Hypothyroidism-Causative Genes Reveals Unexpected Thyroglobulin Gene Variants in Patients with Iodide Transport Defect.International journal of molecular sciences · 2022Article
- The Iodide Transport Defect-Causing Y348D Mutation in the NaThyroid : official journal of the American Thyroid Association · 2021Article
- A Novel SLC5A5 Variant Reveals the Crucial Role of Kinesin Light Chain 2 in Thyroid Hormonogenesis.The Journal of clinical endocrinology and metabolism · 2021Article
- Allosteric regulation of mammalian NaNature structural & molecular biology · 2020Article
- Mapping of Ion and Substrate Binding Sites in Human Sodium Iodide Symporter (hNIS).Journal of chemical information and modeling · 2020Article
- Inter-species variation in monovalent anion substrate selectivity and inhibitor sensitivity in the sodium iodide symporter (NIS).PloS one · 2020Article
- Implications of NaJournal of the Endocrine Society · 2019Review
- A Carboxy-Terminal Monoleucine-Based Motif Participates in the Basolateral Targeting of the Na+/I- Symporter.Endocrinology · 2019Article
- Iodide Binding in Sodium-Coupled Cotransporters.Journal of chemical information and modeling · 2017Article
- Effects of a Phosphoinositide-3-Kinase Inhibitor on Anaplastic Thyroid Cancer Stem CellsAsian Pacific journal of cancer prevention : APJCP · 2017Article
- An extremely high dietary iodide supply forestalls severe hypothyroidism in NaScientific reports · 2017Article
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Authors and funding
7 authors.
Funding
Abstract
The sodium/iodide symporter (NIS) mediates active I(-) transport in the thyroid-the first step in thyroid hormone biosynthesis-with a 2 Na(+): 1 I(-) stoichiometry. The two Na(+) binding sites (Na1 and Na2) and the I(-) binding site interact allosterically: when Na(+) binds to a Na(+) site, the affinity of NIS for the other Na(+) and for I(-) increases significantly. In all Na(+)-dependent transporters with the same fold as NIS, the side chains of two residues, S353 and T354 (NIS numbering), were identified as the Na(+) ligands at Na2. To understand the cooperativity between the substrates, we investigated the coordination at the Na2 site. We determined that four other residues-S66, D191, Q194, and Q263-are also involved in Na(+) coordination at this site. Experiments in whole cells demonstrated that these four residues participate in transport by NIS: mutations at these positions result in proteins that, although expressed at the plasma membrane, transport little or no I(-) These residues are conserved throughout the entire SLC5 family, to which NIS belongs, suggesting that they serve a similar function in the other transporters. Our findings also suggest that the increase in affinity that each site displays when an ion binds to another site may result from changes in the dynamics of the transporter. These mechanistic insights deepen our understanding not only of NIS but also of other transporters, including many that, like NIS, are of great medical relevance.
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