Evidence map›Paper›PMID 26525414›Full record

ArticleMolecular and cellular endocrinology2016

Nuclear import of the thyroid hormone receptor α1 is mediated by importin 7, importin β1, and adaptor importin α1.

Vincent R Roggero, Jibo Zhang, Laura E Parente, Yazdi Doshi, Rose C Dziedzic, Emma L McGregor, Arev D Varjabedian, Sara E Schad, Cornelius Bondzi, Lizabeth A Allison

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular endocrinology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

19 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Subcellular Distribution of Thyroid Hormone Receptor Beta in Ovarian Cancer.International journal of molecular sciences · 2022
    Article
  10. Main Factors Involved in Thyroid Hormone Action.Molecules (Basel, Switzerland) · 2021
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. New insights into thyroid hormone action.Pharmacology & therapeutics · 2017
    Review
  19. Article
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

10 authors at 3 institutions in 1 country.

Vincent R RoggeroDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Jibo ZhangDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Laura E ParenteDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Yazdi DoshiDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Rose C DziedzicDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Emma L McGregorDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Arev D VarjabedianDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Sara E SchadDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA.
Cornelius BondziDepartment of Biological Sciences, Hampton University, Hampton, VA, 23668, USA.
Lizabeth A AllisonDepartment of Biology, College of William and Mary, Williamsburg, VA, 23185, USA. Electronic address: laalli@wm.edu.
William & Mary · USWilliams (United States) · USHampton University · US

Funding

Thyroid Hormone Receptor Mislocalization and PathogenesisR15DK058028 · NIDDK · COLLEGE OF WILLIAM AND MARY · PI ALLISON, LIZABETH A · 2001 to 2022
$1.9M
NIDDK NIH HHS 2R15DK058028-03NIDDK NIH HHS R15 DK058028
6 · The paper itself

Abstract

The thyroid hormone receptor α1 (TRα1) is a nuclear receptor for thyroid hormone that shuttles rapidly between the nucleus and cytoplasm. Our prior studies showed that nuclear import of TRα1 is directed by two nuclear localization signals, one in the N-terminal A/B domain and the other in the hinge domain. Here, we showed using in vitro nuclear import assays that TRα1 nuclear localization is temperature and energy-dependent and can be reconstituted by the addition of cytosol. In HeLa cells expressing green fluorescent protein (GFP)-tagged TRα1, knockdown of importin 7, importin β1 and importin α1 by RNA interference, or treatment with an importin β1-specific inhibitor, significantly reduced nuclear localization of TRα1, while knockdown of other importins had no effect. Coimmunoprecipitation assays confirmed that TRα1 interacts with importin 7, as well as importin β1 and the adapter importin α1, suggesting that TRα1 trafficking into the nucleus is mediated by two distinct pathways.

Indexed as

alpha Karyopherinsbeta KaryopherinsCell NucleusHeLa CellsHumansKaryopherinsProtein TransportQuinazolinesReceptors, Cytoplasmic and NuclearSignal TransductionTemperatureThyroid Hormone Receptors alphaalpha Karyopherinsbeta KaryopherinsimportazoleIPO7 protein, humankaryopherin alpha 2KaryopherinsKPNB1 protein, humanQuinazolinesReceptors, Cytoplasmic and NuclearThyroid Hormone Receptors alphaImportinNuclear importThyroid hormoneThyroid hormone receptor

Identifiers

PMID26525414
PMCPMC4684427
OpenAlexW1948977654

What OpenQuestion holds

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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.