Evidence map›Paper›PMID 20924358›Full record

ArticleThe EMBO journal2010

Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90.

Shan Yan, Xuxu Sun, Binggang Xiang, Hui Cang, Xunlei Kang, Yuying Chen, Hui Li, Guiying Shi, Edward T H Yeh, Beilei Wang and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

69 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
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  6. Review
  7. Review
  8. Article
  9. The SUMOylation and ubiquitination crosstalk in cancer.Journal of cancer research and clinical oncology · 2023
    Review
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  11. Article
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  20. Review

9 more citing papers are in PubMed but not listed here.

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

12 authors at 3 institutions in 2 countries.

Shan YanDepartment of Biochemistry and Cell Biology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, PR China.
Xuxu Sun
Binggang Xiang
Hui Cang
Xunlei Kang
Yuying Chen
Hui Li
Guiying Shi
Edward T H Yeh
Beilei Wang
Xiangrui Wang
Jing Yi
Shanghai Jiao Tong University · CNRenji Hospital · CNThe University of Texas MD Anderson Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular chaperone heat shock protein 90 (Hsp90) and the co-chaperone/ubiquitin ligase carboxyl terminus of Hsc70-interacting protein (CHIP) control the turnover of client proteins. How this system decides to stabilize or degrade the client proteins under particular physiological or pathological conditions is unclear. We report here a novel client protein, the SUMO2/3 protease SENP3, that is sophisticatedly regulated by CHIP and Hsp90. SENP3 is maintained at a low basal level under non-stress condition due to Hsp90-independent CHIP-mediated ubiquitination. Upon mild oxidative stress, SENP3 undergoes thiol modification, which recruits Hsp90. Hsp90/SENP3 association protects SENP3 from CHIP-mediated ubiquitination and subsequent degradation, but this effect of Hsp90 requires the presence of CHIP. Our data demonstrate for the first time that CHIP and Hsp90 interplay with a client alternately under non-stress and stress conditions, and the choice between stabilization and degradation is made by the redox state of the client. In addition, enhanced SENP3/Hsp90 association is found in cancer. These findings provide new mechanistic insight into how cells regulate the SUMO protease in response to oxidative stress.

Indexed as

CysteineCysteine EndopeptidasesEnzyme StabilityHEK293 CellsHeLa CellsHSP90 Heat-Shock ProteinsHumansOxidation-ReductionOxidative StressReactive Oxygen SpeciesUbiquitinationUbiquitin-Protein LigasesCysteineCysteine EndopeptidasesHSP90 Heat-Shock ProteinsReactive Oxygen SpeciesSENP3 protein, humanSTUB1 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID20924358
PMCPMC2989103
OpenAlexW2141829793

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.