Evidence map›Paper›PMID 12865408›Full record

ArticleThe Journal of clinical investigation2003

Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation.

Cyntia Curcio-Morelli, Ann Marie Zavacki, Marcelo Christofollete, Balazs Gereben, Beatriz C G de Freitas, John W Harney, Zaibo Li, Guan Wu, Antonio C Bianco

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Variable transduction of thyroid hormone signaling in structures of the mouse brain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Cryo-EM: A new dawn in thyroid biology.Molecular and cellular endocrinology · 2021
    Review
  9. Article
  10. From Selenium Absorption to Selenoprotein Degradation.Biological trace element research · 2019
    Review
  11. Structural and functional studies of USP20 ZnF-UBP domain by NMR.Protein science : a publication of the Protein Society · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. The Deiodinase Trio and Thyroid Hormone Signaling.Methods in molecular biology (Clifton, N.J.) · 2018
    Review
  17. Review
  18. Article
  19. Review
  20. Article

2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Cyntia Curcio-MorelliDivision of Endocrinology, Brigham and Women's Hospital, Harvard Institutes of Medicine, Boston, Massachusetts 02115, USA.
Ann Marie Zavacki
Marcelo Christofollete
Balazs Gereben
Beatriz C G de Freitas
John W Harney
Zaibo Li
Guan Wu
Antonio C Bianco
Harvard University Press · USUniversity of Rochester · USBrigham and Women's Hospital · USHungarian Academy of Sciences · HU

Funding

SELENODEIODINAS PROCESSING BY THE PROTEASOME SYSTEMR01DK058538 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BIANCO, ANTONIO C, GEREBEN, BALÁZS · 2001 to 2024
$6.0M
Selenodeidinase Processing by the Proteasome SystemR56DK058538 · NIDDK · UNIVERSITY OF CHICAGO · PI BIANCO, ANTONIO C · 2019 to 2019
$203k
NIDDK NIH HHS DK-58538NIDDK NIH HHS R01 DK058538NIDDK NIH HHS R56 DK058538
6 · The paper itself

Abstract

The type 2 iodothyronine deiodinase (D2) is an integral membrane ER-resident selenoenzyme that activates the pro-hormone thyroxine (T4) and supplies most of the 3,5,3'-triiodothyronine (T3) that is essential for brain development. D2 is inactivated by selective conjugation to ubiquitin, a process accelerated by T4 catalysis and essential for the maintenance of T3 homeostasis. A yeast two-hybrid screen of a human-brain library with D2 as bait identified von Hippel-Lindau protein-interacting deubiquitinating enzyme-1 (VDU1). D2 interaction with VDU1 and VDU2, a closely related deubiquitinase, was confirmed in mammalian cells. Both VDU proteins colocalize with D2 in the ER, and their coexpression prolongs D2 half-life and activity by D2 deubiquitination. VDU1, but not VDU2, is markedly increased in brown adipocytes by norepinephrine or cold exposure, further amplifying the increase in D2 activity that results from catecholamine-stimulated de novo synthesis. Thus, deubiquitination regulates the supply of active thyroid hormone to brown adipocytes and other D2-expressing cells.

Indexed as

Tumor Suppressor ProteinsUbiquitin-Protein LigasesAdipocytesAdipose Tissue, BrownBlotting, WesternCatalysisCatecholaminesCell LineEndopeptidasesEndoplasmic ReticulumGene LibraryHumansIodide PeroxidaseIodothyronine Deiodinase Type IILigasesMicroscopy, FluorescenceCatecholaminesEndopeptidasesIodide PeroxidaseIodothyronine Deiodinase Type IILigasesThyroid HormonesThyroxineTriiodothyronineTumor Suppressor ProteinsUbiquitinUbiquitin-Protein LigasesUbiquitin ThiolesteraseUSP20 protein, humanUSP33 protein, humanVHL protein, humanVon Hippel-Lindau Tumor Suppressor Protein

Identifiers

PMID12865408
PMCPMC164294
OpenAlexW2060405471

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.