Evidence map›Paper›PMID 23269275›Full record

ArticleCancer research2013

BRMS1 suppresses lung cancer metastases through an E3 ligase function on histone acetyltransferase p300.

Yuan Liu, Marty W Mayo, Alykhan S Nagji, Emily H Hall, Lisa S Shock, Aizhen Xiao, Edward B Stelow, David R Jones

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Metastasis suppressors: functional pathways.Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  12. Article
  13. Article
  14. Cdk2 regulates metastasis suppressor BRMS1.Cell cycle (Georgetown, Tex.) · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Microenvironmental Influences on Metastasis Suppressor Expression and Function during a Metastatic Cell's Journey.Cancer microenvironment : official journal of the International Cancer Microenvironment Society · 2014
    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

8 authors at 1 institution in 1 country.

Yuan LiuDepartment of Surgery, University of Virginia, Charlottesville, VA 22908, USA.
Marty W Mayo
Alykhan S Nagji
Emily H Hall
Lisa S Shock
Aizhen Xiao
Edward B Stelow
David R Jones
University of Virginia · US

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Thomas P. Loughran · 1987 to 2026
$72.1M
Cancer Research Training Program: From Molecular Mechanisms to Therapeutic StrategiesT32CA009109 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Andrew Carl Dudley, Melanie R Rutkowski · 1985 to 2026
$13.9M
Role of IKK in NSCLC: Modulation of SMRT and NF-kappaBR01CA104397 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI MAYO, MARTY W · 2004 to 2012
$2.4M
Epigenetic and post-translational regulation of the metastasis suppressor BRMS1R01CA136705 · NCI · UNIVERSITY OF VIRGINIA · PI JONES, DAVID R · 2009 to 2013
$1.5M
Inflammatory Cytokines Link NF-kappaB with Bim Degradation and MetastasisR01CA132580 · NCI · UNIVERSITY OF VIRGINIA · PI MAYO, MARTY W · 2008 to 2012
$1.4M
NCI NIH HHS P30 CA044579NCI NIH HHS R01 CA104397NCI NIH HHS R01 CA132580NCI NIH HHS R01 CA136705NCI NIH HHS T32 CA009109
6 · The paper itself

Abstract

The mechanisms through which the metastasis suppressor gene BRMS1 functions are poorly understood. Herein, we report the identification of a previously undescribed E3 ligase function of BRMS1 on the histone acetyltransferase p300. BRMS1 induces polyubiquitination of p300, resulting in its proteasome-mediated degradation. We identify BRMS1 as the first eukaryote structural mimic of the bacterial IpaH E3 ligase family and establish that the evolutionarily conserved CXD motif located in BRMS1 is responsible for its E3 ligase function. Mutation of this E3 ligase motif not only abolishes BRMS1-induced p300 polyubiquitination and degradation, but importantly, dramatically reduces the metastasis suppressor function of BRMS1 in both in vitro and in vivo models of lung cancer metastasis.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternCell LineCell Line, TumorE1A-Associated p300 ProteinGene Expression Regulation, NeoplasticHEK293 CellsHumansLung NeoplasmsMiceMice, NudeMolecular Sequence DataMutationNeoplasm MetastasisNeoplasm ProteinsBRMS1 protein, humanE1A-Associated p300 ProteinEP300 protein, humanNeoplasm ProteinsRepressor ProteinsTumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID23269275
PMCPMC3578176
OpenAlexW2050857920

What OpenQuestion holds

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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.