Evidence map›Paper›PMID 20181954›Full record

ArticleThe Journal of biological chemistry2010

SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress.

Yan Han, Chao Huang, Xuxu Sun, Binggang Xiang, Ming Wang, Edward T H Yeh, Yuying Chen, Hui Li, Guiying Shi, Hui Cang and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

59 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. SENP2 Promotes VSMC Phenotypic Switching via Myocardin De-SUMOylation.International journal of molecular sciences · 2022
    Article
  10. Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases.International journal of molecular sciences · 2022
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. SUMO: From Bench to Bedside.Physiological reviews · 2020
    Review
  16. Article
  17. The requirement of SUMO2/3 for SENP2 mediated extraembryonic and embryonic development.Developmental dynamics : an official publication of the American Association of Anatomists · 2020
    Article
  18. Mild Oxidative Stress Reduces NRF2 SUMOylation to PromoteOxidative medicine and cellular longevity · 2020
    Article
  19. 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

15 authors at 2 institutions in 2 countries.

Yan HanDepartment of Cell Biology, Key Laboratory of the Education Ministry for Cell Differentiation and Apoptosis, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Chao Huang
Xuxu Sun
Binggang Xiang
Ming Wang
Edward T H Yeh
Yuying Chen
Hui Li
Guiying Shi
Hui Cang
Yueping Sun
Jian Wang
Wei Wang
Fei Gao
Jing Yi
Shanghai Jiao Tong University · CNThe University of Texas MD Anderson Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small ubiquitin-like modifier (SUMO) 2/3 is known to conjugate to substrates in response to a variety of cellular stresses. However, whether and how SUMO2/3-specific proteases are involved in de-conjugation under cell stress is unclear. Here, we show that low doses of hydrogen peroxide (H(2)O(2)) induce an increase of the SENP3 protein, which removes SUMO2/3 from promyelocytic leukemia (PML). Low dose H(2)O(2) causes SENP3 to co-localize with PML bodies and reduces the number of PML bodies in a SENP3-dependent manner. Furthermore, de-conjugation of SUMO2/3 from PML is responsible for the accelerated cell proliferation caused by low dose H(2)O(2). Knocking down PML promotes basal cell proliferation as expected. This can be reversed by reconstitution with wild-type PML but not its mutant lacking SUMOylation, indicating that only the SUMOylated PML can play an inhibitory role for cell proliferation. Thus, SENP3 appears to be a key mediator in mild oxidative stress-induced cell proliferation via regulation of the SUMOylation status of PML. Furthermore, SENP3 is over-accumulated in a variety of primary human cancers including colon adenocarcinoma in which PML is hypo-SUMOylated. These results reveal an important role of SENP3 and the SUMOylation status of PML in the regulation of cell proliferation under oxidative stress.

Indexed as

Cell ProliferationOxidative StressAdenocarcinomaAnimalsColonic NeoplasmsCysteine EndopeptidasesDose-Response Relationship, DrugGene Knockdown TechniquesHeLa CellsHumansHydrogen PeroxideMiceNIH 3T3 CellsNuclear ProteinsOxidantsPromyelocytic Leukemia ProteinCysteine EndopeptidasesHydrogen PeroxideNuclear ProteinsOxidantsPML protein, humanPromyelocytic Leukemia ProteinSENP3 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanTranscription FactorsTumor Suppressor ProteinsUbiquitins

Identifiers

PMID20181954
PMCPMC2857110
OpenAlexW2046969377

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.