Evidence map›Paper›PMID 15367689›Full record

ArticleMolecular and cellular biology2004

The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors.

Seema Verma, Ayesha Ismail, Xiuhua Gao, Guilian Fu, Xiaotao Li, Bert W O'Malley, Zafar Nawaz

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 92 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Steroid receptor coactivators as therapeutic targets in the female reproductive system.The Journal of steroid biochemistry and molecular biology · 2015
    Review
  8. Post-translational modifications of the progesterone receptors.The Journal of steroid biochemistry and molecular biology · 2014
    Review
  9. Review
  10. Article
  11. Article
  12. Progesterone and autoimmune disease.Autoimmunity reviews · 2012
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  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

7 authors at 2 institutions in 1 country.

Seema VermaCancer Center, Criss III, Room 352, Creighton University, 2500 California Plaza, Omaha, NE 68178, USA.
Ayesha Ismail
Xiuhua Gao
Guilian Fu
Xiaotao Li
Bert W O'Malley
Zafar Nawaz
Creighton University · USBaylor College of Medicine · US

Funding

REPRODUCTIVE HORMONES: BIOLOGICAL AND MOLECULAR ACTIONSR01HD008188 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI DAVID M LONARD, JOHN P LYDON · 1985 to 2026
$16.3M
NUCLEAR HORMONE ACTION--ROLE OF UBIQUITIN PATHWAYSR01DK056833 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI NAWAZ, ZAFAR · 2000 to 2003
$883k
RAT PUP HUDDLING: INTEGRATING MODELS AND EXPERIMENTSF32HD008188 · NICHD · INDIANA UNIVERSITY BLOOMINGTON · PI SCHANK, JEFFREY C · 1996 to 1998
–
NICHD NIH HHS F32 HD008188NICHD NIH HHS HD-08188NICHD NIH HHS R01 HD008188NIDDK NIH HHS DK56833NIDDK NIH HHS R01 DK056833
6 · The paper itself

Abstract

We investigated the role of the ubiquitin-conjugating enzyme UBCH7 in nuclear receptor transactivation. Using transient transfection assays, we demonstrated that UBCH7 modulates the transcriptional activity of progesterone receptor (PR) and glucocorticoid, androgen, and retinoic acid receptors in a hormone-dependent manner and that the ubiquitin conjugation activity of UBCH7 is required for its ability to potentiate transactivation by steroid hormone receptors (SHR). However, UBCH7 showed no significant effect on the transactivation functions of p53 and VP-16 activation domain. Depletion of endogenous UBCH7 protein by small interfering RNAs suggests that UBCH7 is required for the proper function of SHR. Furthermore, a chromatin immunoprecipitation assay demonstrated the hormone-dependent recruitment of UBCH7 onto estrogen receptor- and PR-responsive promoters. Additionally, we show that UBCH7 and E6-associated protein (E6-AP) synergistically enhance PR transactivation. We also demonstrate that UBCH7 interacts with steroid receptor coactivator 1 (SRC-1) and that UBCH7 coactivation function is dependent on SRC-1. Taken together, our results reveal the possible role of UBCH7 in steroid receptor transactivation and provide insights into the mechanism of action of UBCH7 in receptor function.

Indexed as

Gene Expression RegulationHeLa CellsHistone AcetyltransferasesHumansNuclear Receptor Coactivator 1Promoter Regions, GeneticReceptors, EstrogenReceptors, ProgesteroneReceptors, SteroidTranscription FactorsTranscription, GeneticUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesHistone AcetyltransferasesNCOA1 protein, humanNuclear Receptor Coactivator 1Receptors, EstrogenReceptors, ProgesteroneReceptors, SteroidTranscription FactorsUBE2L3 protein, humanUBE3A protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID15367689
PMCPMC516762
OpenAlexW2144156833

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.