Evidence map›Paper›PMID 20065040›Full record

ArticleMolecular and cellular biology2010

Estrogen receptors recruit SMRT and N-CoR corepressors through newly recognized contacts between the corepressor N terminus and the receptor DNA binding domain.

Natalia Varlakhanova, Chelsea Snyder, Soumia Jose, Johnnie B Hahm, Martin L Privalsky

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.4field-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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. HDAC7 influences ER-⍺ transcription via NCoR-HDAC3 dissociation.Biochimica et biophysica acta. Proteins and proteomics · 2025
    Article
  4. miR-10a/b-5p-NCOR2 Regulates Insulin-Resistant Diabetes in Female Mice.International journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Significance of estrogen receptor subtypes in breast tumorigenesis and progression.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Article
  16. Article
  17. Article
  18. Nuclear receptor corepressor complexes in cancer: mechanism, function and regulation.American journal of clinical and experimental urology · 2014
    Review
  19. Article
  20. 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 1 institution in 1 country.

Natalia VarlakhanovaDepartment of Microbiology, College of Biological Sciences, University of California at Davis, Davis, California 95616, USA.
Chelsea Snyder
Soumia Jose
Johnnie B Hahm
Martin L Privalsky
University of California, Davis · US

Funding

UC Davis MCB T32 Administrative Supplement to Recognize Excellence in Diversity, Equity, Inclusion, and Accessibility (DEIA) MentorshipT32GM007377 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CHEDIN, FREDERIC LOUIS · 1985 to 2023
$9.9M
Role of cofactors in nuclear hormone receptor function.R01DK053528 · NIDDK · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1998 to 2012
$2.9M
NIDDK NIH HHS R01 DK053528NIDDK NIH HHS R01DK53528NIGMS NIH HHS T32 GM007377NIGMS NIH HHS T32-GM007377
6 · The paper itself

Abstract

Estrogen receptors (ERs) are hormone-regulated transcription factors that regulate key aspects of reproduction and development. ERs are unusual in that they do not typically repress transcription in the absence of hormone but instead possess otherwise cryptic repressive functions that are revealed upon binding to certain hormone antagonists. The roles of corepressors in the control of these aspects of ER function are complex and incompletely understood. We report here that ERs recruit SMRT through an unusual mode of interaction involving multiple contact surfaces. Two surfaces of SMRT, located at the N- and C-terminal domains, contribute to the recruitment of the corepressor to ERs in vitro and are crucial for the corepressor modulation of ER transcriptional activity in cells. These corepressor surfaces contact the DNA binding domain of the receptor, rather than the hormone binding domain previously elucidated for other corepressor/nuclear receptor interactions, and are modulated by the ER's recognition of cognate DNA binding sites. Several additional nuclear receptors, and at least one other corepressor, N-CoR, share aspects of this novel mode of corepressor recruitment. Our results highlight a molecular mechanism that helps explain several previously paradoxical aspects of ER-mediated transcriptional antagonism, which may have a broader significance for an understanding of target gene repression by other nuclear receptors.

Indexed as

Amino Acid MotifsAmino Acid SequenceDNAEstradiolEstrogen Receptor alphaHumansLigandsMolecular Sequence DataNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2PPAR alphaProtein BindingProtein Structure, TertiaryReceptor, Farnesoid X-ActivatedReceptors, Cytoplasmic and NuclearReceptors, Thyroid HormoneDNAEstradiolEstrogen Receptor alphaLigandsNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2PPAR alphaReceptor, Farnesoid X-ActivatedReceptors, Cytoplasmic and NuclearReceptors, Thyroid Hormone

Identifiers

PMID20065040
PMCPMC2832498
OpenAlexW2154302028

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.