Evidence map›Paper›PMID 21852228›Full record

ArticleThe Journal of biological chemistry2011

The p73 tumor suppressor is targeted by Pirh2 RING finger E3 ubiquitin ligase for the proteasome-dependent degradation.

Yong-Sam Jung, Yingjuan Qian, Xinbin Chen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Host and Viral Zinc-Finger Proteins in COVID-19.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Review
  8. Spatial and temporal roles of SARS-CoV PLFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Review
  9. Regulating tumor suppressor genes: post-translational modifications.Signal transduction and targeted therapy · 2020
    Review
  10. Review
  11. Regulation of the p53 Family Proteins by the Ubiquitin Proteasomal Pathway.International journal of molecular sciences · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Regulation of Tumor Suppressor p63 by the Ubiquitin-Proteasome System.International journal of molecular sciences · 2016
    Review
  17. Article
  18. p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

3 authors at 1 institution in 1 country.

Yong-Sam JungComparative Oncology Laboratory, University of California, Davis, California 95616.
Yingjuan QianComparative Oncology Laboratory, University of California, Davis, California 95616.
Xinbin ChenComparative Oncology Laboratory, University of California, Davis, California 95616. Electronic address: xbchen@ucdavis.edu.
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
MECHANISM OF P73 DEPENDENT TUMOR SUPPRESSIONR01CA081237 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XINBIN · 1999 to 2022
$6.8M
The role of DNA polymerase eta in DNA damage response and p53 activationR01CA123227 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XINBIN · 2010 to 2014
$1.4M
NCI NIH HHS CA081237NCI NIH HHS CA123227NCI NIH HHS P30 CA093373NCI NIH HHS R01 CA081237NCI NIH HHS R01 CA123227
6 · The paper itself

Abstract

The p73 gene, a homologue of the p53 tumor suppressor, is expressed as TA and ΔN isoforms. TAp73 has similar activity as p53 and functions as a tumor suppressor whereas ΔNp73 has both pro- and anti-survival functions. While p73 is rarely mutated in spontaneous tumors, the expression status of p73 is linked to the sensitivity of tumor cells to chemotherapy and prognosis for many types of human cancer. Thus, uncovering its regulators in tumors is of great interest. Here, we found that Pirh2, a RING finger E3 ubiquitin ligase, promotes the proteasome-dependent degradation of p73. Specifically, we showed that knockdown of Pirh2 up-regulates, whereas ectopic expression of Pirh2 down-regulates, expression of endogenous and exogenous p73. In addition, Pirh2 physically associates with and promotes TAp73 polyubiquitination both in vivo and in vitro. Moreover, we found that p73 can be degraded by both 20 S and 26 S proteasomes. Finally, we showed that Pirh2 knockdown leads to growth suppression in a TAp73-dependent manner. Taken together, our findings indicate that Pirh2 promotes the proteasomal turnover of TAp73, and thus targeting Pirh2 to restore TAp73-mediated growth suppression in p53-deficient tumors may be developed as a novel anti-cancer strategy.

Indexed as

Gene Expression Regulation, NeoplasticCell Line, TumorDNA-Binding ProteinsGene Knockdown TechniquesHumansMutationNeoplasmsNuclear ProteinsProteasome Endopeptidase ComplexTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor ProteinsUbiquitin-Protein Ligasesdelta Np73 protein, humanDNA-Binding ProteinsNuclear ProteinsProteasome Endopeptidase ComplexRCHY1 protein, humanTP53 protein, humanTP73 protein, humanTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID21852228
PMCPMC3195599
OpenAlexW2026513625

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.