Evidence map›Paper›PMID 22614022›Full record

ArticleOncogene2013

Cross-talk between phosphorylation and SUMOylation regulates transforming activities of an adenoviral oncoprotein.

P Wimmer, P Blanchette, S Schreiner, W Ching, P Groitl, J Berscheminski, P E Branton, H Will, T Dobner

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Viral Interplay with the Host Sumoylation System.Advances in experimental medicine and biology · 2017
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  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

9 authors at 2 institutions in 2 countries.

P WimmerDepartment of Molecular Virology, Heinrich-Pette-Institute-Leibniz-Institute for Experimental Virology, Hamburg, Germany.
P Blanchette
S Schreiner
W Ching
P Groitl
J Berscheminski
P E Branton
H Will
T Dobner
Leibniz Institute of Virology (LIV) · DEMcGill University · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Since the discovery of post-translational modification (PTM) by the small ubiquitin-related modifiers (SUMOs), a multitude of proteins have been described to be reversibly modified, resulting in the alteration of several cellular pathways. Interestingly, various pathogens gain access to this modification system, although the molecular mechanisms and functional consequences are barely understood. We show here that the adenoviral oncoprotein E1B-55K is a substrate of the SUMO conjugation system, which is directly linked to its C-terminal phosphorylation. This regulative connection is indispensable for modulation of the tumor suppressor p53/chromatin-remodeling factor Daxx by E1B-55K and, consequently, its oncogenic potential in primary mammalian cells. In virus infection, E1B-55K PTMs are necessary for localization to viral transcription/replication sites. Furthermore, we identify the E2 enzyme Ubc9 as an interaction partner of E1B-55K, providing a possible molecular explanation for SUMO-dependent modulation of cellular target proteins. In conclusion, these results for the first time provide evidence how E1B-55K PTMs are regulated and subsequently facilitate exploitation of the host cell SUMOylation machinery.

Indexed as

Adaptor Proteins, Signal TransducingAdenoviridaeAmino Acid SequenceAnimalsAnimals, NewbornCells, CulturedCell Transformation, NeoplasticCo-Repressor ProteinsHEK293 CellsHumansModels, BiologicalMolecular ChaperonesMolecular Sequence DataNuclear ProteinsPhosphorylationPhylogenyAdaptor Proteins, Signal TransducingCo-Repressor ProteinsDAXX protein, humanE1B55K protein, adenovirusMolecular ChaperonesNuclear ProteinsProtein KinasesTumor Suppressor Protein p53Viral Proteins

Identifiers

PMID22614022
OpenAlexW2038479442

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.