Allosteric regulation of mammalian Na+/I- symporter activity by perchlorate

Nat Struct Mol Biol. 2020 Jun;27(6):533-539. doi: 10.1038/s41594-020-0417-5. Epub 2020 May 25.

Abstract

The Na+/I- symporter (NIS), the plasma membrane protein that actively transports I- (stoichiometry 2Na+:1I-) in thyroid physiology and radioiodide-based thyroid cancer treatment, also transports the environmental pollutant perchlorate (stoichiometry 1Na+:1ClO4-), which competes with I- for transport. Until now, the mechanism by which NIS transports different anion substrates with different stoichiometries has remained unelucidated. We carried out transport measurements and analyzed these using a statistical thermodynamics-based equation and electrophysiological experiments to show that the different stoichiometry of ClO4- transport is due to ClO4- binding to a high-affinity non-transport allosteric site that prevents Na+ from binding to one of its two sites. Furthermore, low concentrations of ClO4- inhibit I- transport not only by competition but also, critically, by changing the stoichiometry of I- transport to 1:1, which greatly reduces the driving force. The data reveal that ClO4- pollution in drinking water is more dangerous than previously thought.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Allosteric Regulation
  • Allosteric Site
  • Animals
  • Anions / chemistry
  • Anions / metabolism
  • Binding Sites
  • Biological Transport
  • Dogs
  • Electrophysiology / methods
  • Female
  • Humans
  • Iodine / metabolism
  • Madin Darby Canine Kidney Cells
  • Mutation
  • Oocytes / metabolism
  • Oocytes / physiology
  • Perchlorates / chemistry
  • Perchlorates / metabolism*
  • Rats
  • Sodium / metabolism
  • Symporters / chemistry*
  • Symporters / genetics
  • Symporters / metabolism*
  • Thermodynamics
  • Xenopus laevis

Substances

  • Anions
  • Perchlorates
  • Symporters
  • sodium-iodide symporter
  • Iodine
  • Sodium
  • perchlorate