Evidence map›Paper›PMID 23650190›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2013

Asn441 plays a key role in folding and function of the Na+/I- symporter (NIS).

Wenjing Li, Juan Pablo Nicola, L Mario Amzel, Nancy Carrasco

Open access · bronzeAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.9field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Silent but Not Harmless: A SynonymousFrontiers in endocrinology · 2022
    Article
  6. The Iodide Transport Defect-Causing Y348D Mutation in the NaThyroid : official journal of the American Thyroid Association · 2021
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Implications of NaJournal of the Endocrine Society · 2019
    Review
  12. Defects of Thyroid Hormone Synthesis and Action.Endocrinology and metabolism clinics of North America · 2017
    Review
  13. Review
  14. 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
    Article
  15. Sodium/Iodide Symporter Mutant V270E Causes Stunted Growth but No Cognitive Deficiency.The Journal of clinical endocrinology and metabolism · 2015
    Article
  16. Article
  17. Article
  18. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Wenjing LiDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York, USA.
Juan Pablo Nicola
L Mario Amzel
Nancy Carrasco
Yale University · USAlbert Einstein College of Medicine · USJohns Hopkins Medicine · US

Funding

THYROID SODIUM I/ SYMPORTERR01DK041544 · NIDDK · YESHIVA UNIVERSITY · PI ABBOTT, GEOFFREY W, CARRASCO, NANCY · 1989 to 2017
$5.6M
NIDDK NIH HHS DK-41544NIDDK NIH HHS R01 DK041544
6 · The paper itself

Abstract

The Na(+)/I(-) symporter (NIS) is a plasma membrane glycoprotein that mediates active I(-) transport in the thyroid, the first step in the biosynthesis of the iodine-containing thyroid hormones T3 and T4. Several NIS mutants have been identified as a cause of congenital I(-) transport defect (ITD), and their investigation has yielded valuable mechanistic information on NIS. Here we report a thorough characterization of the ITD-causing NIS mutation in which the sixth intracellular loop residues 439-443 are missing. This mutant protein was intracellularly retained, incompletely glycosylated, and intrinsically inactive. Engineering 5 Ala at positions 439-443 partially recovered cell surface targeting and activity (∼15%). Strikingly, NIS with the sequence 439-AANAA-443, in which Asn was restored at position 441, was targeted to the plasma membrane and exhibited ∼95% the transport activity of WT NIS. Based on our NIS homology model, we propose that the side chain of N441, a residue conserved throughout most of the SLC5 family, interacts with the main chain amino group of G444, capping the α-helix of transmembrane segment XII and thus stabilizing the structure of the molecule. Our data provide insight into a critical interhelical interaction required for NIS folding and activity.

Indexed as

Protein FoldingAmino Acid SequenceAnimalsAsparagineBinding SitesBiological TransportCell LineCell MembraneChlorocebus aethiopsCOS CellsHumansImmunoblottingIodineMicroscopy, ConfocalModels, MolecularMolecular Sequence DataAsparagineIodineSodium-Iodide SymportersSymporterscongenital hypothyroidismhelix cappinginterhelical interactionplasma membrane targetingprotein folding

Identifiers

PMID23650190
PMCPMC3714583
OpenAlexW2076327239

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.