Evidence map›Paper›PMID 20569464›Full record

ArticleMolecular cancer2010

Deletion analysis of BMI1 oncoprotein identifies its negative regulatory domain.

Ajay K Yadav, Anagh A Sahasrabuddhe, Manjari Dimri, Prashant V Bommi, Rachana Sainger, Goberdhan P Dimri

Open access · goldAbstract read
In one paragraph

Article in Molecular cancer, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. p53 Inhibits Bmi-1-driven Self-Renewal and Defines Salivary Gland Cancer Stemness.Clinical cancer research : an official journal of the American Association for Cancer Research · 2022
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. BMI1, a new target of CK2α.Molecular cancer · 2017
    Article
  14. Article
  15. Article
  16. 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

6 authors at 2 institutions in 2 countries.

Ajay K YadavDepartment of Medicine, NorthShore University HealthSystem Research Institute, Evanston, IL 60201, USA.
Anagh A Sahasrabuddhe
Manjari Dimri
Prashant V Bommi
Rachana Sainger
Goberdhan P Dimri
NorthShore University HealthSystem · USUniversity of Delhi · IN

Funding

The role of BMI1 in breast cancerR01CA094150 · NCI · NORTHSHORE UNIV HEALTHSYSTEM RES INST · PI DIMRI, GOBERDHAN P · 2003 to 2013
$2.7M
NCI NIH HHS R01 CA094150
6 · The paper itself

Abstract

backgroundThe polycomb group (PcG) protein BMI1 is an important regulator of development. Additionally, aberrant expression of BMI1 has been linked to cancer stem cell phenotype and oncogenesis. In particular, its overexpression has been found in several human malignancies including breast cancer. Despite its established role in stem cell maintenance, cancer and development, at present not much is known about the functional domains of BMI1 oncoprotein. In the present study, we carried out a deletion analysis of BMI1 to identify its negative regulatory domain.

resultsWe report that deletion of the C-terminal domain of BMI1, which is rich in proline-serine (PS) residues and previously described as PEST-like domain, increased the stability of BMI1, and promoted its pro-oncogenic activities in human mammary epithelial cells (HMECs). Specifically, overexpression of a PS region deleted mutant of BMI1 increased proliferation of HMECs and promoted an epithelial-mesenchymal transition (EMT) phenotype in the HMECs. Furthermore, when compared to the wild type BMI1, exogenous expression of the mutant BMI1 led to a significant downregulation of p16INK4a and an efficient bypass of cellular senescence in human diploid fibroblasts.

conclusionsIn summary, our data suggest that the PS domain of BMI1 is involved in its stability and that it negatively regulates function of BMI1 oncoprotein. Our results also suggest that the PS domain of BMI1 could be targeted for the treatment of proliferative disorders such as cancer and aging.

Indexed as

Regulatory Sequences, Nucleic AcidCell LineEpithelial-Mesenchymal TransitionHalf-LifeHumansNuclear ProteinsPolycomb Repressive Complex 1Proto-Oncogene ProteinsRepressor ProteinsSequence DeletionBMI1 protein, humanNuclear ProteinsPolycomb Repressive Complex 1Proto-Oncogene ProteinsRepressor Proteins

Identifiers

PMID20569464
PMCPMC2900245
OpenAlexW2131548177

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.