Evidence map›Paper›PMID 29895970›Full record

ArticleOncogene2018

TRPS1 regulates oestrogen receptor binding and histone acetylation at enhancers.

A A Serandour, H Mohammed, A Miremadi, K W Mulder, J S Carroll

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2018. 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
1.0field-weighted citation impact, top 24% 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, 43 citations in OpenAlex.

  1. Pathogenesis and potential therapeutic targets of trichorhinophalangeal syndrome; lessons obtained from animal studies.Developmental dynamics : an official publication of the American Association of Anatomists · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. A dysfunctional miR-1-TRPS1-MYOG axis drives ERMS by suppressing terminal myogenic differentiation.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

5 authors at 2 institutions in 2 countries.

A A SerandourCambridge Institute, Cancer Research UK, University of Cambridge, Robinson Way, Cambridge, CB2 0RE, UK.
H MohammedCambridge Institute, Cancer Research UK, University of Cambridge, Robinson Way, Cambridge, CB2 0RE, UK.
A MiremadiCambridge Institute, Cancer Research UK, University of Cambridge, Robinson Way, Cambridge, CB2 0RE, UK.
K W MulderCambridge Institute, Cancer Research UK, University of Cambridge, Robinson Way, Cambridge, CB2 0RE, UK. k.mulder@science.ru.nl.
J S CarrollCambridge Institute, Cancer Research UK, University of Cambridge, Robinson Way, Cambridge, CB2 0RE, UK. jason.carroll@cruk.cam.ac.uk.
Cancer Research UK · GBUniversity of Cambridge · GB

Funding

Cancer Research UK 20411European Research Council 242664
6 · The paper itself

Abstract

The chromatin state is finely tuned to regulate function and specificity for transcription factors such as oestrogen receptor alpha (ER), which contributes to cell growth in breast cancer. ER transcriptional potential is mediated, in large part, by the specific associated proteins and co-factors that interact with it. Despite the identification and characterisation of several ER coregulators, a complete and systematic view of ER-regulating chromatin modifiers is lacking. By exploiting a focused siRNA screen that investigated the requirement for a library of 330 chromatin regulators in ER-mediated cell growth, we find that the NuRD and coREST histone deacetylation complexes are critical for breast cancer cell proliferation. Further, by proteomic and genomics approaches, we discover the transcription factor TRPS1 to be a key interactor of the NuRD and coREST complexes. Interestingly, TRPS1 gene amplification occurs in 28% of human breast tumours and is associated with poor prognosis. We propose that TRPS1 is required to repress spurious binding of ER, where it contributes to the removal of histone acetylation. Our data suggest that TRPS1 is an important ER-associated transcriptional repressor that regulates cell proliferation, chromatin acetylation and ER binding at the chromatin of cis-regulatory elements.

Indexed as

AcetylationBreast NeoplasmsCell Line, TumorCo-Repressor ProteinsDNA-Binding ProteinsFemaleGene Expression Regulation, NeoplasticHistonesHumansMi-2 Nucleosome Remodeling and Deacetylase ComplexNerve Tissue ProteinsReceptors, EstrogenRepressor ProteinsTranscriptional ActivationTranscription FactorsCo-Repressor ProteinsDNA-Binding ProteinsHistonesMi-2 Nucleosome Remodeling and Deacetylase ComplexNerve Tissue ProteinsRCOR1 protein, humanReceptors, EstrogenRepressor ProteinsTranscription FactorsTRPS1 protein, human

Identifiers

PMID29895970
PMCPMC6169732
OpenAlexW2808281859

What OpenQuestion holds

Textmetadata
LicenceTDM
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.