Evidence map›Paper›PMID 34711683›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Calcineurin regulates the stability and activity of estrogen receptor α.

Takahiro Masaki, Makoto Habara, Yuki Sato, Takahiro Goshima, Keisuke Maeda, Shunsuke Hanaki, Midori Shimada

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Calcineurin in cancer signaling networks.Nagoya journal of medical science · 2025
    Review
  5. Article
  6. Review
  7. Calcineurin-mediated dephosphorylation stabilizes E2F1 protein by suppressing binding of the FBXW7 ubiquitin ligase subunit.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Adenosine receptors in breast cancer.Molecular biology reports · 2024
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. FKBP52 and FKBP51 differentially regulate the stability of estrogen receptor in breast cancer.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Review
  18. Review
  19. Review
  20. Review
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.

Takahiro MasakiDepartment of Biochemistry, Joint Faculty of Veterinary Science, Yamaguchi University, Yamaguchi 753-8511, Japan.ORCID 0000-0002-2948-0277
Makoto HabaraDepartment of Biochemistry, Joint Faculty of Veterinary Science, Yamaguchi University, Yamaguchi 753-8511, Japan.ORCID 0000-0001-6418-1291
Yuki SatoDepartment of Biochemistry, Joint Faculty of Veterinary Science, Yamaguchi University, Yamaguchi 753-8511, Japan.
Takahiro GoshimaDepartment of Cell Biology, Graduate School of Medical Sciences, Nagoya City University, Nagoya 467-8601, Japan.
Keisuke MaedaDepartment of Biochemistry, Joint Faculty of Veterinary Science, Yamaguchi University, Yamaguchi 753-8511, Japan.
Shunsuke HanakiDepartment of Biochemistry, Joint Faculty of Veterinary Science, Yamaguchi University, Yamaguchi 753-8511, Japan.
Midori ShimadaDepartment of Biochemistry, Joint Faculty of Veterinary Science, Yamaguchi University, Yamaguchi 753-8511, Japan; shimada@yamaguchi-u.ac.jp.ORCID 0000-0002-2718-8600
Yamaguchi University · JPNagoya City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Estrogen receptor α (ER-α) mediates estrogen-dependent cancer progression and is expressed in most breast cancer cells. However, the molecular mechanisms underlying the regulation of the cellular abundance and activity of ER-α remain unclear. We here show that the protein phosphatase calcineurin regulates both ER-α stability and activity in human breast cancer cells. Calcineurin depletion or inhibition down-regulated the abundance of ER-α by promoting its polyubiquitination and degradation. Calcineurin inhibition also promoted the binding of ER-α to the E3 ubiquitin ligase E6AP, and calcineurin mediated the dephosphorylation of ER-α at Ser

Indexed as

Breast NeoplasmsCalcineurinCell Line, TumorEstradiolEstrogen Receptor alphaEstrogensFemaleGene ExpressionGene Expression Regulation, NeoplasticHumansProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalReceptors, EstrogenUbiquitinUbiquitinationUbiquitin-Protein LigasesCalcineurinESR1 protein, humanEstradiolEstrogen Receptor alphaEstrogensPPP3CA protein, humanProteasome Endopeptidase ComplexReceptors, EstrogenUBE3A protein, humanUbiquitinUbiquitin-Protein Ligasesbreast cancercalcineurinestrogen receptorαubiquitination

Identifiers

PMID34711683
PMCPMC8612228
OpenAlexW3210206897

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.