Evidence map›Paper›PMID 27174643›Full record

ArticleThe EMBO journal2016

Redox regulation of SUMO enzymes is required for ATM activity and survival in oxidative stress.

Nicolas Stankovic-Valentin, Katarzyna Drzewicka, Cornelia König, Elmar Schiebel, Frauke Melchior

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. SUMO Antibody Validation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Article
  6. Knocking Down PIAS3 Reduces HCell biochemistry and biophysics · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. The SUMO Pathway in Hematomalignancies and Their Response to Therapies.International journal of molecular sciences · 2019
    Review
  18. 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

5 authors at 1 institution in 1 country.

Nicolas Stankovic-ValentinZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH) Heidelberg University DKFZ - ZMBH Alliance, Heidelberg, Germany.
Katarzyna DrzewickaZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH) Heidelberg University DKFZ - ZMBH Alliance, Heidelberg, Germany.
Cornelia KönigZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH) Heidelberg University DKFZ - ZMBH Alliance, Heidelberg, Germany.
Elmar SchiebelZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH) Heidelberg University DKFZ - ZMBH Alliance, Heidelberg, Germany.
Frauke MelchiorZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH) Heidelberg University DKFZ - ZMBH Alliance, Heidelberg, Germany f.melchior@zmbh.uni-heidelberg.de.ORCID 0000-0001-9546-8797
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To sense and defend against oxidative stress, cells depend on signal transduction cascades involving redox-sensitive proteins. We previously identified SUMO (small ubiquitin-related modifier) enzymes as downstream effectors of reactive oxygen species (ROS). Hydrogen peroxide transiently inactivates SUMO E1 and E2 enzymes by inducing a disulfide bond between their catalytic cysteines. How important their oxidation is in light of many other redox-regulated proteins has however been unclear. To selectively disrupt this redox switch, we identified a catalytically fully active SUMO E2 enzyme variant (Ubc9 D100A) with strongly reduced propensity to maintain a disulfide with the E1 enzyme in vitro and in cells. Replacement of Ubc9 by this variant impairs cell survival both under acute and mild chronic oxidative stresses. Intriguingly, Ubc9 D100A cells fail to maintain activity of the ATM-Chk2 DNA damage response pathway that is induced by hydrogen peroxide. In line with this, these cells are also more sensitive to the ROS-producing chemotherapeutic drugs etoposide/Vp16 and Ara-C. These findings reveal that SUMO E1~E2 oxidation is an essential redox switch in oxidative stress.

Indexed as

Gene Expression RegulationOxidative StressProtein Processing, Post-TranslationalStress, PhysiologicalCell LineCell SurvivalDisulfidesHumansMutant ProteinsOxidation-ReductionUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9DisulfidesMutant ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9ATMoxidative stressredox regulationSUMOUbc9

Identifiers

PMID27174643
PMCPMC4867669
OpenAlexW2392525692

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.