Evidence map›Paper›PMID 11792840›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Supervillin associates with androgen receptor and modulates its transcriptional activity.

Huei-Ju Ting, Shuyuan Yeh, Kazuo Nishimura, Chawnshang Chang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

37 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Androgens as the "old age stick" in skeletal muscle.Cell communication and signaling : CCS · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. An emerging link between LIM domain proteins and nuclear receptors.Cellular and molecular life sciences : CMLS · 2018
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Sphingosine kinase 1 isoform-specific interactions in breast cancer.Molecular endocrinology (Baltimore, Md.) · 2014
    Article
  17. Review
  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

4 authors at 2 institutions in 1 country.

Huei-Ju TingGeorge Whipple Laboratory for Cancer Research, Department of Pathology, and the Cancer Center, University of Rochester, Rochester, NY 14642, USA.
Shuyuan Yeh
Kazuo Nishimura
Chawnshang Chang
University of Rochester · USUniversity of Wisconsin–Madison · US

Funding

NCI NIH HHS CA71570
6 · The paper itself

Abstract

Activation of androgen receptor (AR) via androgen in muscle cells has been closely linked to their growth and differentiation. Here, we report the cloning and characterization of supervillin (SV), a 205-kDa actin-binding protein, as an AR coregulator from the skeletal muscle cDNA library. Mammalian two-hybrid and glutathione S-transferase pull-down assays indicate a domain within SV (amino acids 594-1268) can interact with AR N terminus and DNA-binding domain-ligand-binding domain in a ligand-enhanced manner. Subcellular colocalization studies with fluorescence staining indicate SV can colocalize with AR in the presence of 5 alpha-dihydrotestosterone in COS-1 cells. The functional reporter assays showed full-length SV and the SV peptide (amino acids 831-1281) within the interaction domain can enhance AR transactivation. Furthermore, SV can enhance the endogenous AR target gene, p27(KIP1), expression in prostate PC-3(AR2) cells. SV preferentially enhanced AR rather than other tested nuclear receptors and could be induced by natural androgens better than other steroids. SV can also cooperate with other AR coregulators, such as ARA55 or ARA70, to enhance AR transactivation further. Unlike SRC-1 that can enhance the interaction between AR N terminus and AR C terminus, SV shows a mild suppressive effect on N-C interactions, suggesting SV may go through a different mechanism to enhance AR transactivation. Together, our data demonstrate that SV is an AR coregulator that can enhance AR transactivation in muscle and other cells.

Indexed as

AnimalsBinding SitesCell LineCell NucleusHumansMembrane ProteinsMicrofilament ProteinsMuscle, SkeletalProtein Structure, TertiaryReceptors, AndrogenRecombinant Fusion ProteinsTranscriptional ActivationTransfectionTwo-Hybrid System TechniquesMembrane ProteinsMicrofilament ProteinsReceptors, AndrogenRecombinant Fusion ProteinsSVIL protein, human

Identifiers

PMID11792840
PMCPMC117362
OpenAlexW2009666412

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.