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TitleStructural insights into the mechanism of the sodium/iodide symporter.
Journal, issue, pagesNature, Vol. 612, Issue 7941, Page 795-801, Year 2022
Publish dateDec 14, 2022
AuthorsSilvia Ravera / Juan Pablo Nicola / Glicella Salazar-De Simone / Fred J Sigworth / Erkan Karakas / L Mario Amzel / Mario A Bianchet / Nancy Carrasco /
PubMed AbstractThe sodium/iodide symporter (NIS) is the essential plasma membrane protein that mediates active iodide (I) transport into the thyroid gland, the first step in the biosynthesis of the thyroid hormones- ...The sodium/iodide symporter (NIS) is the essential plasma membrane protein that mediates active iodide (I) transport into the thyroid gland, the first step in the biosynthesis of the thyroid hormones-the master regulators of intermediary metabolism. NIS couples the inward translocation of I against its electrochemical gradient to the inward transport of Na down its electrochemical gradient. For nearly 50 years before its molecular identification, NIS was the molecule at the centre of the single most effective internal radiation cancer therapy: radioiodide (I) treatment for thyroid cancer. Mutations in NIS cause congenital hypothyroidism, which must be treated immediately after birth to prevent stunted growth and cognitive deficiency. Here we report three structures of rat NIS, determined by single-particle cryo-electron microscopy: one with no substrates bound; one with two Na and one I bound; and one with one Na and the oxyanion perrhenate bound. Structural analyses, functional characterization and computational studies show the substrate-binding sites and key residues for transport activity. Our results yield insights into how NIS selects, couples and translocates anions-thereby establishing a framework for understanding NIS function-and how it transports different substrates with different stoichiometries and releases substrates from its substrate-binding cavity into the cytosol.
External linksNature / PubMed:36517601 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.3 Å
Structure data

26806

7uuy

EMDB-26806, PDB-7uuy:
Structure of the sodium/iodide symporter (NIS)
Method: EM (single particle) / Resolution: 3.3 Å

26807

7uuz

EMDB-26807, PDB-7uuz:
Structure of the sodium/iodide symporter (NIS) in complex with perrhenate and sodium
Method: EM (single particle) / Resolution: 3.2 Å

26808

7uv0

EMDB-26808, PDB-7uv0:
Structure of the sodium/iodide symporter (NIS) in complex with iodide and sodium
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-3PH:
1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE

ChemComp-NA:
Unknown entry

ChemComp-REO:
PERRHENATE

ChemComp-IOD:
IODIDE ION

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSPORT PROTEIN / NIS / iodide / symporter / cryo-EM

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