Evidence map›Paper›PMID 23395904›Full record

ArticleThe EMBO journal2013

Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response.

Yung-Lin Hsieh, Hong-Yi Kuo, Che-Chang Chang, Mandar T Naik, Pei-Hsin Liao, Chun-Chen Ho, Tien-Chi Huang, Jen-Chong Jeng, Pang-Hung Hsu, Ming-Daw Tsai and 2 more

Abstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.7field-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

39 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. SUMOylation targeting mitophagy in cardiovascular diseases.Journal of molecular medicine (Berlin, Germany) · 2022
    Review
  6. Review
  7. Review
  8. SUMO: From Bench to Bedside.Physiological reviews · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. A role for S-nitrosylation of the SUMO-conjugating enzyme SCE1 in plant immunity.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Ubc9 overexpression and SUMO1 deficiency blunt inflammation after intestinal ischemia/reperfusion.Laboratory investigation; a journal of technical methods and pathology · 2018
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 1 country.

Yung-Lin HsiehInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, ROC.
Hong-Yi Kuo
Che-Chang Chang
Mandar T Naik
Pei-Hsin Liao
Chun-Chen Ho
Tien-Chi Huang
Jen-Chong Jeng
Pang-Hung Hsu
Ming-Daw Tsai
Tai-Huang Huang
Hsiu-Ming Shih
Institute of Biomedical Sciences, Academia Sinica · TWNational Taiwan University · TWInstitute of Biological Chemistry, Academia Sinica · TWNational Defense Medical Center · TWNational Taiwan Ocean University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While numerous small ubiquitin-like modifier (SUMO) conjugated substrates have been identified, very little is known about the cellular signalling mechanisms that differentially regulate substrate sumoylation. Here, we show that acetylation of SUMO E2 conjugase Ubc9 selectively downregulates the sumoylation of substrates with negatively charged amino acid-dependent sumoylation motif (NDSM) consisting of clustered acidic residues located downstream from the core ψ-K-X-E/D consensus motif, such as CBP and Elk-1, but not substrates with core ψ-K-X-E/D motif alone or SUMO-interacting motif. Ubc9 is acetylated at residue K65 and K65 acetylation attenuates Ubc9 binding to NDSM substrates, causing a reduction in NDSM substrate sumoylation. Furthermore, Ubc9 K65 acetylation can be downregulated by hypoxia via SIRT1, and is correlated with hypoxia-elicited modulation of sumoylation and target gene expression of CBP and Elk-1 and cell survival. Our data suggest that Ubc9 acetylation/deacetylation serves as a dynamic switch for NDSM substrate sumoylation and we report a previously undescribed SIRT1/Ubc9 regulatory axis in the modulation of protein sumoylation and the hypoxia response.

Indexed as

Protein Processing, Post-TranslationalAcetylationAcetyltransferasesCell HypoxiaCells, Culturedets-Domain Protein Elk-1HCT116 CellsHEK293 CellsHeLa CellsHumansRNA, Small InterferingSirtuin 1SUMO-1 ProteinSumoylationUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Acetyltransferasesets-Domain Protein Elk-1RNA, Small InterferingSIRT1 protein, humanSirtuin 1SUMO-1 ProteinUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID23395904
PMCPMC3604730
OpenAlexW2137198943

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.