Evidence map›Paper›PMID 20078863›Full record

ArticleBMC molecular biology2010

The transforming acidic coiled coil (TACC1) protein modulates the transcriptional activity of the nuclear receptors TR and RAR.

Romain Guyot, Séverine Vincent, Julie Bertin, Jacques Samarut, Patrick Ravel-Chapuis

Open access · hybridAbstract read
In one paragraph

Article in BMC molecular biology, 2010. 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
0.8field-weighted citation impact, top 28% 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, 29 citations in OpenAlex.

  1. Article
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  7. Transcriptomic Context ofBiomedicines · 2023
    Article
  8. Review
  9. Article
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  11. Review
  12. Article
  13. Diencephalic Size Is Restricted by a Novel Interplay Between GCN5 Acetyltransferase Activity and Retinoic Acid Signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  14. Article
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  19. 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

5 authors at 3 institutions in 1 country.

Romain GuyotInstitut de Génomique Fonctionnelle de Lyon, Universitéde Lyon, Université Lyon 1, CNRS, INRA, Ecole Normale Supérieure de Lyon, 46 allée d'Italie, 69364 Lyon Cedex 07, France.
Séverine Vincent
Julie Bertin
Jacques Samarut
Patrick Ravel-Chapuis
Université Claude Bernard Lyon 1 · FRCentre National de la Recherche Scientifique · FRInstitut de Génomique Fonctionnelle de Lyon · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe transcriptional activity of Nuclear hormone Receptors (NRs) is regulated by interaction with coactivator or corepressor proteins. Many of these cofactors have been shown to have a misregulated expression or to show a subcellular mislocalization in cancer cell lines or primary tumors. Therefore they can be factors involved in the process of oncogenesis.

resultsWe describe a novel NR coregulator, TACC1, which belongs to the Transforming Acidic Coiled Coil (TACC) family. The interaction of TACC1 with Thyroid Hormone Receptors (TR) and several other NRs has been shown in a yeast two-hybrid screen and confirmed by GST pulldown, colocalization and co-immunoprecipitation experiments. TACC1 interacts preferentially with unliganded NRs. In F9 cells, endogenous TACC1 localized in the chromatin-enriched fraction of the nucleus and interacted with Retinoid Acid Receptors (RARalpha) in the nucleus. TACC1 depletion in the cell led to decreased RARalpha and TRalpha ligand-dependent transcriptional activity and to delocalization of TR from the nucleus to the cytoplasm.

conclusionsFrom these experimental studies we propose that TACC1 might be a scaffold protein building up a transcriptional complex around the NRs we studied. This function of TACC1 might account for its involvement in several forms of tumour development.

Indexed as

AnimalsCell LineCell NucleusFetal ProteinsHumansMiceMicrotubule-Associated ProteinsMutationNuclear ProteinsProtein BindingReceptors, Retinoic AcidRetinoic Acid Receptor alphaThyroid Hormone Receptors alphaTwo-Hybrid System TechniquesFetal ProteinsMicrotubule-Associated ProteinsNuclear ProteinsRARA protein, humanRara protein, mouseReceptors, Retinoic AcidRetinoic Acid Receptor alphaTACC1 protein, humanThyroid Hormone Receptors alpha

Identifiers

PMID20078863
PMCPMC2822774
OpenAlexW2077052802

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.