Evidence map›Paper›PMID 32786121›Full record

ArticleJournal of cellular biochemistry2021

The SUMO-specific protease SENP1 deSUMOylates p53 and regulates its activity.

Krishna M Chauhan, Yingxiao Chen, Yiyi Chen, Andrew T Liu, Xiao-Xin Sun, Mu-Shui Dai

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023
    Review
  6. Review
  7. Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Deciphering the PTM codes of the tumor suppressor p53.Journal of molecular cell biology · 2022
    Review
  10. SUMOylation and NEDDylation in Primary and Metastatic Cancers to Bone.Frontiers in cell and developmental biology · 2022
    Review
  11. Review
  12. Review
  13. Article
  14. 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

6 authors at 1 institution in 1 country.

Krishna M ChauhanDepartment of Molecular and Medical Genetics, School of Medicine, Oregon Health & Science University, Portland, Oregon.
Yingxiao ChenDepartment of Molecular and Medical Genetics, School of Medicine, Oregon Health & Science University, Portland, Oregon.
Yiyi ChenBiostatistics Program, School of Public Health, Oregon Health & Science University, Portland, Oregon.
Andrew T LiuDepartment of Molecular and Medical Genetics, School of Medicine, Oregon Health & Science University, Portland, Oregon.
Xiao-Xin SunDepartment of Molecular and Medical Genetics, School of Medicine, Oregon Health & Science University, Portland, Oregon.
Mu-Shui DaiDepartment of Molecular and Medical Genetics, School of Medicine, Oregon Health & Science University, Portland, Oregon.ORCID 0000-0001-9031-6962
Oregon Health & Science University · US

Funding

Hydroxylation regulation of c-MycR01CA186241 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI Mu-Shui Dai, ROSALIE C SEARS · 2015 to 2026
$4.2M
Role of Otubain 1 in the p53 PathwayR01CA160474 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI DAI, MU-SHUI · 2012 to 2016
$1.6M
Novel roles for USP36 in ribosome biogenesisR01GM130604 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI DAI, MU-SHUI · 2019 to 2022
$1.2M
NCI NIH HHS R01 CA160474NCI NIH HHS R01 CA186241NIGMS NIH HHS R01 GM130604
6 · The paper itself

Abstract

The stability and activity of the p53 tumor suppressor protein are tightly regulated by various posttranslational modifications, including SUMOylation. p53 can be modified by both SUMO1 and SUMO2, although how SUMOylation regulates p53 activity is still obscure. Whether p53 activity is directly regulated by deSUMOylation is also unclear. Here, we show that SENP1, a SUMO-specific protease implicated in pro-oncogenic roles, is a p53 deSUMOylating enzyme. SENP1 interacts with p53 and deSUMOylates p53 in cells and in vitro. Knockdown of SENP1 markedly induced p53 transactivation activity. We further show that SENP1 depletion synergizes with DNA damage-inducing agent etoposide to induce p53 activation and the expression of p21, leading to synergistic growth inhibition of cancer cells. Our results reveal that SENP1 is a critical p53 deSUMOylating enzyme and a promising therapeutic target in wild-type p53 containing cancer cells.

Indexed as

Cysteine EndopeptidasesDNA DamageEtoposideHumansProtein Processing, Post-TranslationalSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinTumor Suppressor Protein p53Cysteine EndopeptidasesEtoposideSENP1 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO2 protein, humanTumor Suppressor Protein p53p53SENP1SUMOSUMO proteaseSUMOylation

Identifiers

PMID32786121
PMCPMC7802976
OpenAlexW3049699154

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.