Evidence map›Paper›PMID 16135815›Full record

ArticleMolecular and cellular biology2005

Rapid estrogen-induced phosphorylation of the SRC-3 coactivator occurs in an extranuclear complex containing estrogen receptor.

Fuzhong F Zheng, Ray-Chang Wu, Carolyn L Smith, Bert W O'Malley

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  7. Article
  8. Review
  9. Review
  10. Article
  11. Cancer Stem Cell Phenotypes in ERMolecular cancer research : MCR · 2018
    Article
  12. Endocrine-disrupting chemicals and fatty liver disease.Nature reviews. Endocrinology · 2017
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

4 authors at 1 institution in 1 country.

Fuzhong F ZhengMolecular and Cellular Biology, One Baylor Plaza, Houston, TX 77030, USA.
Ray-Chang Wu
Carolyn L Smith
Bert W O'Malley
Baylor College of Medicine · US

Funding

ESTROGEN RECEPTOR-COREGULATOR FUNCTIONAL INTERACTIONSR01DK053002 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI SMITH, CAROLYN LOUISE · 1997 to 2018
$4.7M
NICHD NIH HHS HD08818NIDDK NIH HHS DK53002NIDDK NIH HHS R01 DK053002
6 · The paper itself

Abstract

SRC-3/AIB1/ACTR/pCIP/RAC3/TRAM1 is a primary transcriptional coregulator for estrogen receptor (ER). Six SRC-3 phosphorylation sites have been identified, and these can be induced by steroids, cytokines, and growth factors, involving multiple kinase signaling pathways. Using phosphospecific antibodies for six phosphorylation sites, we investigated the mechanisms involved in estradiol (E2)-induced SRC-3 phosphorylation and found that this occurs only when either activated estrogen receptor alpha (ERalpha) or activated ERbeta is present. Both the activation function 1 and the ligand binding domains of ERalpha are required for maximal induction. Mutations in the coactivator binding groove of the ERalpha ligand binding domain inhibit E2-stimulated SRC-3 phosphorylation, as do mutations in the nuclear receptor-interacting domain of SRC-3, suggesting that ERalpha must directly contact SRC-3 for this posttranslational modification to take place. A transcriptionally inactive ERalpha mutant which localizes to the cytoplasm supports E2-induced SRC-3 phosphorylation. Mutations of the ERalpha DNA binding domain did not block this rapid E2-dependent SRC-3 phosphorylation. Together these data demonstrate that E2-induced SRC-3 phosphorylation is dependent on a direct interaction between SRC-3 and ERalpha and can occur outside of the nucleus. Our results provide evidence for an early nongenomic action of ER on SRC-3 that supports the well-established downstream genomic roles of estrogen and coactivators.

Indexed as

AcetyltransferasesAmino Acid MotifsAntibodies, Phospho-SpecificCell NucleusCytoplasmDNAEstradiolEstrogen Receptor alphaEstrogen Receptor betaHistone AcetyltransferasesHumansMutationNuclear ProteinsNuclear Receptor Coactivator 3Oncogene ProteinsPhosphorylationAcetyltransferasesAntibodies, Phospho-SpecificDNAEstradiolEstrogen Receptor alphaEstrogen Receptor betaHistone AcetyltransferasesIFNGR2 protein, humanNCOA3 protein, humanNuclear ProteinsNuclear Receptor Coactivator 3Oncogene ProteinsReceptors, InterferonSelective Estrogen Receptor ModulatorsTrans-Activators

Identifiers

PMID16135815
PMCPMC1234335
OpenAlexW2097130643

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.