Evidence map›Paper›PMID 31293051›Full record

ArticleMolecular oncology2019

p32 is a negative regulator of p53 tetramerization and transactivation.

Nikhil Baban Ghate, Jinman Kim, Yonghwan Shin, Alan Situ, Tobias S Ulmer, Woojin An

Open access · goldAbstract read
In one paragraph

Article in Molecular oncology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Spatial multiomics profiling reveals ZFP36-mediated immunometabolic reprogramming in bladder cancer.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Identification of a Novel Oncogenic Fusion GeneInternational journal of molecular sciences · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. 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 1 institution in 1 country.

Nikhil Baban GhateDepartment of Biochemistry and Molecular Medicine, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA, USA.
Jinman KimDepartment of Biochemistry and Molecular Medicine, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA, USA.
Yonghwan ShinDepartment of Biochemistry and Molecular Medicine, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA, USA.
Alan SituDepartment of Biochemistry and Molecular Medicine, Zilkha Neurogenetic Institute, University of Southern California, Los Angeles, CA, USA.
Tobias S UlmerDepartment of Biochemistry and Molecular Medicine, Zilkha Neurogenetic Institute, University of Southern California, Los Angeles, CA, USA.
Woojin AnDepartment of Biochemistry and Molecular Medicine, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA, USA.ORCID 0000-0001-8756-595X
University of Southern California · US

Funding

Role of histone kinase VprBP in gene silencing: mechanisms, targets, and regulationR01CA201561 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI AN, WOOJIN · 2016 to 2020
$1.9M
NCI NIH HHS R01 CA201561
6 · The paper itself

Abstract

p53 is a sequence-specific transcription factor, and proper regulation of p53 transcriptional activity is critical for orchestrating different tumor-suppressive mechanisms. p32 is a multifunctional protein which interacts with a large number of viral proteins and transcription factors. Here, we investigate the effect of p32 on p53 transactivation and identify a novel mechanism by which p32 alters the functional characteristics of p53. Specifically, p32 attenuates p53-dependent transcription through impairment of p53 binding to its response elements on target genes. Upon p32 expression, p53 levels bound at target genes are decreased, and p53 target genes are inactivated, strongly indicating that p32 restricts p53 occupancy and function at target genes. The primary mechanism contributing to the observed action of p32 is the ability of p32 to interact with the p53 tetramerization domain and to block p53 tetramerization, which in turn enhances nuclear export and degradation of p53, leading to defective p53 transactivation. Collectively, these data establish p32 as a negative regulator of p53 function and suggest the therapeutic potential of targeting p32 for cancer treatment.

Indexed as

Gene Expression Regulation, NeoplasticProtein MultimerizationResponse ElementsTranscriptional ActivationCarrier ProteinsCell Line, TumorHumansMitochondrial ProteinsNeoplasmsTumor Suppressor Protein p53C1QBP protein, humanCarrier ProteinsMitochondrial ProteinsTumor Suppressor Protein p53nuclear export signalp32p53tetramerizationtranscription

Identifiers

PMID31293051
PMCPMC6717765
OpenAlexW2961656322

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.