Evidence map›Paper›PMID 24920999›Full record

ReviewWorld journal of biological chemistry2014

Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1.

Xiao-Xin Sun, Mu-Shui Dai

Open access · diamondAbstract readReview
In one paragraph

Review in World journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 2 pooled it
2.5field-weighted citation impact, top 10% 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, 2 syntheses or guidelines pooled it, 54 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. InvestigatingInternational journal of molecular sciences · 2024
    Article
  9. Potential Otubain1 Inhibitor, an Approach for a Treatment against Breast Cancer.International journal of molecular and cellular medicine · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Molecular Mechanisms of DUBs Regulation in Signaling and Disease.International journal of molecular sciences · 2021
    Review
  20. 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

2 authors at 1 institution in 1 country.

Xiao-Xin SunXiao-Xin Sun, Mu-Shui Dai, Department of Molecular and Medical Genetics, School of Medicine, and the OHSU Knight Cancer Institute, Oregon Health and Science University, Portland, OR 97239, United States.
Mu-Shui DaiXiao-Xin Sun, Mu-Shui Dai, Department of Molecular and Medical Genetics, School of Medicine, and the OHSU Knight Cancer Institute, Oregon Health and Science University, Portland, OR 97239, United States.
Oregon Health & Science University · US

Funding

Role of Otubain 1 in the p53 PathwayR01CA160474 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI DAI, MU-SHUI · 2012 to 2016
$1.6M
Dissection of the feedback inhibition of c-Myc by L11R00CA127134 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI DAI, MU-SHUI · 2009 to 2011
$740k
NCI NIH HHS R00 CA127134NCI NIH HHS R01 CA160474
6 · The paper itself

Abstract

Deubiquitination has emerged as an important mechanism of p53 regulation. A number of deubiquitinating enzymes (DUBs) from the ubiquitin-specific protease family have been shown to regulate the p53-MDM2-MDMX networks. We recently reported that Otub1, a DUB from the OTU-domain containing protease family, is a novel p53 regulator. Interestingly, Otub1 abrogates p53 ubiquitination and stabilizes and activates p53 in cells independently of its deubiquitinating enzyme activity. Instead, it does so by inhibiting the MDM2 cognate ubiquitin-conjugating enzyme (E2) UbcH5. Otub1 also regulates other biological signaling through this non-canonical mechanism, suppression of E2, including the inhibition of DNA-damage-induced chromatin ubiquitination. Thus, Otub1 evolves as a unique DUB that mainly suppresses E2 to regulate substrates. Here we review the current progress made towards the understanding of the complex regulation of the p53 tumor suppressor pathway by DUBs, the biological function of Otub1 including its positive regulation of p53, and the mechanistic insights into how Otub1 suppresses E2.

Indexed as

ApoptosisCell cycleDeubiquitinating enzymesMDM2Otub1p53Ubiquitination

Identifiers

PMID24920999
PMCPMC4050119
OpenAlexW1606354726

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.