Evidence map›Paper›PMID 19304659›Full record

ArticleThe Journal of biological chemistry2009

Mechanism of sustained activation of ribosomal S6 kinase (RSK) and ERK by kaposi sarcoma-associated herpesvirus ORF45: multiprotein complexes retain active phosphorylated ERK AND RSK and protect them from dephosphorylation.

Ersheng Kuang, Fayi Wu, Fanxiu Zhu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

48 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Microcystin-LR activates serine/threonine kinases and alters the phosphoproteome in human HepaRG cells.Toxicon : official journal of the International Society on Toxinology · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Characterization of BoHV-4 ORF45.Frontiers in microbiology · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. A case of convergent evolution: Several viral and bacterial pathogens hijack RSK kinases through a common linear motif.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Human DNA Virus Exploitation of the MAPK-ERK Cascade.International journal of molecular sciences · 2019
    Review
  19. Article
  20. Prostaglandin EAmerican journal of physiology. Lung cellular and molecular physiology · 2019
    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

3 authors at 1 institution in 1 country.

Ersheng KuangDepartment of Biological Science, Florida State University, Tallahassee, Florida 32306-4370.
Fayi WuDepartment of Biological Science, Florida State University, Tallahassee, Florida 32306-4370.
Fanxiu ZhuDepartment of Biological Science, Florida State University, Tallahassee, Florida 32306-4370. Electronic address: fzhu@bio.fsu.edu.
Florida State University · US

Funding

Role of KSHV ORF45 in Viral Immune Evasion &ReplicationR01DE016680 · NIDCR · UNIVERSITY OF PENNSYLVANIA · PI ZHU, FANXIU · 2005 to 2015
$2.5M
NIDCR NIH HHS R01 DE016680NIDCR NIH HHS R01DE016680
6 · The paper itself

Abstract

As obligate intracellular parasites, viruses exploit diverse cellular signaling machineries, including the mitogen-activated protein-kinase pathway, during their infections. We have demonstrated previously that the open reading frame 45 (ORF45) of Kaposi sarcoma-associated herpesvirus interacts with p90 ribosomal S6 kinases (RSKs) and strongly stimulates their kinase activities ( Kuang, E., Tang, Q., Maul, G. G., and Zhu, F. (2008) J. Virol. 82, 1838-1850 ). Here, we define the mechanism by which ORF45 activates RSKs. We demonstrated that binding of ORF45 to RSK increases the association of extracellular signal-regulated kinase (ERK) with RSK, such that ORF45, RSK, and ERK formed high molecular mass protein complexes. We further demonstrated that the complexes shielded active pERK and pRSK from dephosphorylation. As a result, the complex-associated RSK and ERK were activated and sustained at high levels. Finally, we provide evidence that this mechanism contributes to the sustained activation of ERK and RSK in Kaposi sarcoma-associated herpesvirus lytic replication.

Indexed as

Cell LineHerpesvirus 8, HumanHumansImmediate-Early ProteinsMitogen-Activated Protein Kinase KinasesMultiprotein ComplexesRibosomal Protein S6 Kinases, 90-kDaVirus ReplicationImmediate-Early ProteinsMitogen-Activated Protein Kinase KinasesMultiprotein ComplexesORF45 protein, Kaposi's sarcoma-associated herpesvirusRibosomal Protein S6 Kinases, 90-kDa

Identifiers

PMID19304659
PMCPMC2679495
OpenAlexW2100227161

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.