Evidence map›Paper›PMID 22331460›Full record

ArticleCancer research2012

Dmp1 physically interacts with p53 and positively regulates p53's stability, nuclear localization, and function.

Donna P Frazier, Robert D Kendig, Fumitake Kai, Dejan Maglic, Takayuki Sugiyama, Rachel L Morgan, Elizabeth A Fry, Sarah J Lagedrost, Guangchao Sui, Kazushi Inoue

Abstract read
In one paragraph

Article in Cancer research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Identification of DMP1 as Novel p53 Repressed Transcriptional Target.International journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Survival of Lung Cancer Patients Dependent on the LOH Status forInternational journal of molecular sciences · 2020
    Article
  10. c-MYB and DMTF1 in Cancer.Cancer investigation · 2019
    Review
  11. Translocations involving ETS family proteins in human cancer.Integrative cancer science and therapeutics · 2018
    Article
  12. CASP9 germline mutation in a family with multiple brain tumors.Brain pathology (Zurich, Switzerland) · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Transcription factors that interact with p53 and Mdm2.International journal of cancer · 2016
    Review
  20. Novel Molecular Markers for Breast Cancer.Biomarkers in cancer · 2016
    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

10 authors at 1 institution in 1 country.

Donna P FrazierDepartment of Pathology and Cancer Biology, and Graduate Program in Molecular Medicine, Wake Forest University Health Sciences, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA.
Robert D Kendig
Fumitake Kai
Dejan Maglic
Takayuki Sugiyama
Rachel L Morgan
Elizabeth A Fry
Sarah J Lagedrost
Guangchao Sui
Kazushi Inoue
Wake Forest University · US

Funding

Training Program in Cancer BiologyT32CA079448 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI KRIDEL, STEVEN J. · 2000 to 2014
$6.5M
Roles of DMP1 in Ras signaling and lung cancerR01CA106314 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI SUI, GUANGCHAO · 2004 to 2013
$2.6M
NCI NIH HHS 2R01CA106314NCI NIH HHS 5T32CA079448NCI NIH HHS BC100907NCI NIH HHS R01 CA106314NCI NIH HHS T32 CA079448PHS HHS KG080179
6 · The paper itself

Abstract

The transcription factor Dmp1 is a Ras/HER2-activated haplo-insufficient tumor suppressor that activates the Arf/p53 pathway of cell-cycle arrest. Recent evidence suggests that Dmp1 may activate p53 independently of Arf in certain cell types. Here, we report findings supporting this concept with the definition of an Arf-independent function for Dmp1 in tumor suppression. We found that Dmp1 and p53 can interact directly in mammalian cells via the carboxyl-terminus of p53 and the DNA-binding domain of Dmp1. Expression of Dmp1 antagonized ubiquitination of p53 by Mdm2 and promoted nuclear localization of p53. Dmp1-p53 binding significantly increased the level of p53, independent of the DNA-binding activity of Dmp1. Mechanistically, p53 target genes were activated synergistically by the coexpression of Dmp1 and p53 in p53(-/-);Arf(-/-) cells, and genotoxic responses of these genes were hampered more dramatically in Dmp1(-/-) and p53(-/-) cells than in Arf(-/-) cells. Together, our findings identify a robust new mechanism of p53 activation mediated by direct physical interaction between Dmp1 and p53.

Indexed as

Active Transport, Cell NucleusAnimalsBinding SitesCell NucleusCells, CulturedCyclin-Dependent Kinase Inhibitor p16HumansMiceMice, Inbred C57BLProto-Oncogene Proteins c-mdm2Transcription FactorsTranscription, GeneticTumor Suppressor Protein p53UbiquitinationCdkn2a protein, mouseCyclin-Dependent Kinase Inhibitor p16DMTF1 protein, humanDmtf1 protein, mouseProto-Oncogene Proteins c-mdm2Transcription FactorsTumor Suppressor Protein p53

Identifiers

PMID22331460
PMCPMC3319807
OpenAlexW2102680618

What OpenQuestion holds

Textmetadata
LicenceTDM
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.