Evidence map›Paper›PMID 11884601›Full record

ArticleMolecular and cellular biology2002

Protein kinase A associates with HA95 and affects transcriptional coactivation by Epstein-Barr virus nuclear proteins.

Innoc Han, Yong Xue, Shizuko Harada, Sigurd Orstavik, Bjorn Skalhegg, Elliott Kieff

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  9. Review
  10. Epstein-Barr virus nuclear antigen leader protein localizes to promoters and enhancers with cell transcription factors and EBNA2.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. Article
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  16. Article
  17. Epstein-Barr nuclear antigen leader protein coactivates transcription through interaction with histone deacetylase 4.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  18. RNAs induced by Epstein-Barr virus nuclear antigen 2 in lymphoblastoid cell lines.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
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  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

6 authors at 2 institutions in 3 countries.

Innoc HanEwha Institute of Neuroscience, Ewha University Medical School, Seoul 110-783, Korea.
Yong Xue
Shizuko Harada
Sigurd Orstavik
Bjorn Skalhegg
Elliott Kieff
Brigham and Women's Hospital · USUniversity of Oslo · NO

Funding

VIRUS AND CELL GENE EXPRESSION IN KAPOSI SARCOMA ASSOCIATED HERPESVIRUS TUMORSP01CA087661 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 2000 to 2004
$10.9M
Epstein-Barr Virus LMP-1 Mediated OncongenicityR01CA085180 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI KIEFF, ELLIOTT D · 2000 to 2016
$10.6M
NCI NIH HHS CA47008NCI NIH HHS CA85180NCI NIH HHS CA87661NCI NIH HHS P01 CA087661NCI NIH HHS R01 CA085180
6 · The paper itself

Abstract

HA95, a nuclear protein homologous to AKAP95, has been identified in immune precipitates of the Epstein-Barr virus (EBV) coactivating nuclear protein EBNA-LP from EBV-transformed lymphoblastoid cells (LCLs). We now find that HA95 and EBNA-LP are highly associated in LCLs and in B-lymphoma cells where EBNA-LP is expressed by gene transfer. Binding was also evident in yeast two-hybrid assays. HA95 binds to the EBNA-LP repeat domain that is the principal coactivator of transcription. EBNA-LP localizes with HA95 and causes HA95 to partially relocalize with EBNA-LP in promyelocytic leukemia nuclear bodies. Protein kinase A catalytic subunit alpha (PKAcsalpha) is significantly associated with HA95 in the presence or absence of EBNA-LP. Although EBNA-LP is not a PKA substrate, HA95 or PKAcsalpha expression in B lymphoblasts specifically down-regulates the strong coactivating effects of EBNA-LP. The inhibitory effects of PKAcsalpha are reversed by coexpression of protein kinase inhibitor. PKAcsalpha also inhibits EBNA-LP coactivation with the EBNA-2 acidic domain fused to the Gal4 DNA binding domain. Furthermore, EBNA-LP- and EBNA-2-induced expression of the EBV oncogene, LMP1, is down-regulated by PKAcsalpha or HA95 expression in EBV-infected lymphoblasts. These experiments indicate that HA95 and EBNA-LP localize PKAcsalpha at nuclear sites where it can affect transcription from specific promoters. The role of HA95 as a scaffold for transcriptional regulation is discussed.

Indexed as

Intracellular Signaling Peptides and ProteinsTranscriptional ActivationTranscription, GeneticCarrier ProteinsCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsEpstein-Barr Virus Nuclear AntigensHumansModels, GeneticNuclear ProteinsOpen Reading FramesPromoter Regions, GeneticProtein BindingProtein Structure, TertiaryRepetitive Sequences, Amino AcidTumor Cells, CulturedAKAP8L protein, humanCarrier ProteinsCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsEBNA-2 protein, Human herpesvirus 4EBNA-LP protein, Human herpesvirus 4EBV-associated membrane antigen, Epstein-Barr virusEpstein-Barr Virus Nuclear AntigensIntracellular Signaling Peptides and ProteinsNuclear Proteinsprotein kinase modulatorViral Matrix ProteinsViral Proteins

Identifiers

PMID11884601
PMCPMC133669
OpenAlexW2164516553

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.