Evidence map›Paper›PMID 15220438›Full record

ArticleJournal of virology2004

Phosphorylation of Epstein-Barr virus ZEBRA protein at its casein kinase 2 sites mediates its ability to repress activation of a viral lytic cycle late gene by Rta.

Ayman S El-Guindy, George Miller

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.5field-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

32 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Predicting CK2 beta-dependent substrates using linear patterns.Biochemistry and biophysics reports · 2015
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

2 authors at 1 institution in 1 country.

Ayman S El-GuindyDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520-8064, USA.
George Miller
Yale University · US

Funding

VIRAL SMALL RNPS--ROLES IN CELL TRANSFORMATIONP01CA016038 · NCI · YALE UNIVERSITY · PI DIMAIO, DANIEL C. · 1985 to 2020
$25.6M
STUDIES OF EPSTEIN-BARR VIRUSR37CA012055 · NCI · YALE UNIVERSITY · PI MILLER, I. GEORGE · 1989 to 2012
$4.4M
STUDIES OF EPSTEIN-BARR VIRUSR01CA012055 · NCI · YALE UNIVERSITY · PI MILLER, I. GEORGE · 1985 to 2002
$737k
NCI NIH HHS CA12055NCI NIH HHS CA16038NCI NIH HHS P01 CA016038NCI NIH HHS R01 CA012055NCI NIH HHS R37 CA012055
6 · The paper itself

Abstract

ZEBRA, a member of the bZIP family, serves as a master switch between latent and lytic cycle Epstein-Barr virus (EBV) gene expression. ZEBRA influences the activity of another viral transactivator, Rta, in a gene-specific manner. Some early lytic cycle genes, such as BMRF1, are activated in synergy by ZEBRA and Rta. However, ZEBRA suppresses Rta's ability to activate a late gene, BLRF2. Here we show that this repressive activity is dependent on the phosphorylation state of ZEBRA. We find that two residues of ZEBRA, S167 and S173, that are phosphorylated by casein kinase 2 (CK2) in vitro are also phosphorylated in vivo. Inhibition of ZEBRA phosphorylation at the CK2 substrate motif, either by serine-to-alanine substitutions or by use of a specific inhibitor of CK2, abolished ZEBRA's capacity to repress Rta activation of the BLRF2 gene, but did not alter its ability to initiate the lytic cycle or to synergize with Rta in activation of the BMRF1 early-lytic-cycle gene. These studies illustrate how the phosphorylation state of a transcriptional activator can modulate its behavior as an activator or repressor of gene expression. Phosphorylation of ZEBRA at its CK2 sites is likely to play an essential role in proper temporal control of the EBV lytic life cycle.

Indexed as

Gene Expression Regulation, ViralCasein Kinase IICell Line, TumorDNA-Binding ProteinsHerpesvirus 4, HumanHumansImmediate-Early ProteinsMutationPhosphorylationProtein Serine-Threonine KinasesTrans-ActivatorsTranscription, GeneticViral ProteinsVirus ReplicationBRLF1 protein, Human herpesvirus 4BZLF1 protein, Herpesvirus 4, HumanCasein Kinase IIDNA-Binding ProteinsImmediate-Early ProteinsProtein Serine-Threonine KinasesTrans-ActivatorsViral Proteins

Identifiers

PMID15220438
PMCPMC434091
OpenAlexW2145224727

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.