Evidence map›Paper›PMID 23504328›Full record

ArticleThe Journal of biological chemistry2013

Role of RNF4 in the ubiquitination of Rta of Epstein-Barr virus.

Ya-Chun Yang, Yushi Yoshikai, Shih-Wei Hsu, Hisato Saitoh, Li-Kwan Chang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Regulation of Epstein-Barr Virus Minor Capsid Protein BORF1 by TRIM5α.International journal of molecular sciences · 2022
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Less Cytotoxic Protoflavones as Antiviral Agents: Protoapigenone 1'-International journal of molecular sciences · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Viral Interplay with the Host Sumoylation System.Advances in experimental medicine and biology · 2017
    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

5 authors at 2 institutions in 2 countries.

Ya-Chun YangDepartment of Biochemical Science and Technology, College of Life Science, National Taiwan University, Taipei, 106, Taiwan.
Yushi Yoshikai
Shih-Wei Hsu
Hisato Saitoh
Li-Kwan Chang
National Taiwan University · TWKumamoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epstein-Barr virus (EBV) encodes a transcription factor, Rta, which is required to activate the transcription of EBV lytic genes. This study demonstrates that treating P3HR1 cells with a proteasome inhibitor, MG132, causes the accumulation of SUMO-Rta and promotes the expression of EA-D. GST pulldown and coimmunoprecipitation studies reveal that RNF4, a RING-domain-containing ubiquitin E3 ligase, interacts with Rta. RNF4 also targets SUMO-2-conjugated Rta and promotes its ubiquitination in vitro. Additionally, SUMO interaction motifs in RNF4 are important to the ubiquitination of Rta because the RNF4 mutant with a mutation at the motifs eliminates ubiquitination. The mutation of four lysine residues on Rta that abrogated SUMO-3 conjugation to Rta also decreases the enhancement of the ubiquitination of Rta by RNF4. This finding demonstrates that RNF4 is a SUMO-targeted ubiquitin E3 ligase of Rta. Finally, knockdown of RNF4 enhances the expression of Rta and EA-D, subsequently promoting EBV lytic replication and virions production. Results of this study significantly contribute to efforts to elucidate a SUMO-targeted ubiquitin E3 ligase that regulates Rta ubiquitination to influence the lytic development of EBV.

Indexed as

UbiquitinationAmino Acid MotifsCell LineEpstein-Barr Virus InfectionsGene Knockdown TechniquesHerpesvirus 4, HumanHumansImmediate-Early ProteinsMutationNuclear ProteinsSmall Ubiquitin-Related Modifier ProteinsTrans-ActivatorsTranscription FactorsUbiquitinsVirus ReplicationBRLF1 protein, Human herpesvirus 4Immediate-Early ProteinsNuclear ProteinsRNF4 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanTrans-ActivatorsTranscription FactorsUbiquitinsDNA VirusesE3 Ubiquitin LigaseEpstein-Barr VirusProtein DegradationRNF4RtaSumoylationUbiquitination

Identifiers

PMID23504328
PMCPMC3642330
OpenAlexW2079420190

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.