Evidence map›Paper›PMID 21510985›Full record

ArticleVirus research2011

HPV E6 proteins target Ubc9, the SUMO conjugating enzyme.

Phillip R Heaton, Adeline F Deyrieux, Xue-Lin Bian, Van G Wilson

Abstract read
In one paragraph

Article in Virus research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. SUMOylation and Viral Infections of the Brain.Pathogens (Basel, Switzerland) · 2022
    Review
  7. SUMOylation in Viral Replication and Antiviral Defense.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  8. Article
  9. Review
  10. SUMO: a novel target for anti-coronavirus therapy.Pathogens and global health · 2021
    Review
  11. SUMO: From Bench to Bedside.Physiological reviews · 2020
    Review
  12. Article
  13. Viral manipulation of the cellular sumoylation machinery.Cell communication and signaling : CCS · 2017
    Review
  14. Article
  15. Viral Interplay with the Host Sumoylation System.Advances in experimental medicine and biology · 2017
    Review
  16. Article
  17. Article
  18. Identification of sumoylated proteins in the silkworm Bombyx mori.International journal of molecular sciences · 2014
    Article
  19. Review
  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

4 authors at 1 institution in 1 country.

Phillip R HeatonDepartment of Microbial and Molecular Pathogenesis, College of Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114, USA.
Adeline F Deyrieux
Xue-Lin Bian
Van G Wilson
Texas A&M Health Science Center · US

Funding

Cellular Regulation of Papillomavirus E1 FunctionR01CA089298 · NCI · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI WILSON, VAN G. · 2003 to 2007
$1.4M
NCI NIH HHS CA089298NCI NIH HHS R01 CA089298
6 · The paper itself

Abstract

The human papillomavirus oncogenic protein, E6, interacts with a number of cellular proteins, and for some targets, E6 directs their degradation through the ubiquitin-proteasome pathway. Post-translational modification with ubiquitin-like modifiers, such as SUMO, also influences protein activities, protein-protein interactions, and protein stability. We report that the high risk HPVE6 proteins reduce the intracellular quantity of the sole SUMO conjugation enzyme, Ubc9, concomitant with decreased host sumoylation. E6 did not significantly influence transcription of Ubc9, indicating that the effects were likely at the protein level. Consistent with typical E6-mediated proteasomal degradation, E6 bound to Ubc9 in vitro, and required E6AP for reduction of Ubc9 levels. Under stable E6 expression conditions in differentiating keratinocytes there was a decrease in Ubc9 and a loss of numerous sumoylated targets indicating a significant perturbation of the normal sumoylation profile. While E6 is known to inhibit PIASy, a SUMO ligase, our results suggest that HPV E6 also targets the Ubc9 protein to modulate host cell sumoylation, suggesting that the sumoylation system may be an important target during viral reproduction and possibly the subsequent development of cervical cancer.

Indexed as

Cell LineDNA-Binding ProteinsHumansKeratinocytesOncogene Proteins, ViralPapillomaviridaeProtein BindingProtein Interaction MappingRepressor ProteinsTranscription, GeneticUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Virulence FactorsDNA-Binding ProteinsE6 protein, Human papillomavirus type 16E6 protein, Human papillomavirus type 18E6 protein, Human papillomavirus type 6Oncogene Proteins, ViralRepressor ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Virulence Factors

Identifiers

PMID21510985
PMCPMC3103646
OpenAlexW2109560748

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.