Evidence map›Paper›PMID 21680517›Full record

ArticleJournal of virology2011

E6 and E7 from human papillomavirus type 16 cooperate to target the PDZ protein Na/H exchange regulatory factor 1.

Rosita Accardi, Rosa Rubino, Mariafrancesca Scalise, Tarik Gheit, Naveed Shahzad, Miranda Thomas, Lawrence Banks, Cesare Indiveri, Bakary S Sylla, Rosa A Cardone and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

41 citing papers in PubMed, 66 citations in OpenAlex.

  1. Trial
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  6. Genome composition-based deep learning predicts oncogenic potential of HPVs.Frontiers in cellular and infection microbiology · 2024
    Article
  7. Review
  8. Review
  9. Article
  10. HPV16 Impacts NHERF2 Expression in Oropharyngeal Cancers.Pathogens (Basel, Switzerland) · 2023
    Article
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  13. Review
  14. Review
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  16. Review
  17. New roles of the NaAmerican journal of physiology. Renal physiology · 2020
    Review
  18. Review
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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

12 authors at 4 institutions in 2 countries.

Rosita AccardiInfections and Cancer Biology Group, International Agency for Research on Cancer, World Health Organization, France.
Rosa Rubino
Mariafrancesca Scalise
Tarik Gheit
Naveed Shahzad
Miranda Thomas
Lawrence Banks
Cesare Indiveri
Bakary S Sylla
Rosa A Cardone
Stephan J Reshkin
Massimo Tommasino
Centre International de Recherche sur le Cancer · FRInternational Centre for Genetic Engineering and Biotechnology · ITUniversity of Bari Aldo Moro · ITUniversity of Calabria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous studies have shown that the PDZ-binding motif of the E6 oncoprotein from the mucosal high-risk (HR) human papillomavirus (HPV) types plays a key role in HPV-mediated cellular transformation in in vitro and in vivo experimental models. HR HPV E6 oncoproteins have the ability to efficiently degrade members of the PDZ motif-containing membrane-associated guanylate kinase (MAGUK) family; however, it is possible that other PDZ proteins are also targeted by E6. Here, we describe a novel interaction of HPV type 16 (HPV16) E6 with a PDZ protein, Na(+)/H(+) exchange regulatory factor 1 (NHERF-1), which is involved in a number of cellular processes, including signaling and transformation. HPV16 E6 associates with and promotes the degradation of NHERF-1, and this property is dependent on the C-terminal PDZ-binding motif of E6. Interestingly, HPV16 E7, via the activation of the cyclin-dependent kinase complexes, promoted the accumulation of a phosphorylated form of NHERF-1, which is preferentially targeted by E6. Thus, both oncoproteins appear to cooperate in targeting NHERF-1. Notably, HPV18 E6 is not able to induce NHERF-1 degradation, indicating that this property is not shared with E6 from all HR HPV types. Downregulation of NHERF-1 protein levels was also observed in HPV16-positive cervical cancer-derived cell lines, such as SiHa and CaSki, as well as HPV16-positive cervical intraepithelial neoplasia (CIN). Finally, our data show that HPV16-mediated NHERF-1 degradation correlates with the activation of the phosphatidylinositol-3'-OH kinase (PI3K)/AKT signaling pathway, which is known to play a key role in carcinogenesis.

Indexed as

PhosphoproteinsSodium-Hydrogen ExchangersAnimalsGene SilencingHEK293 CellsHuman papillomavirus 16HumansImmunoblottingMiceNIH 3T3 CellsOncogene Proteins, ViralPapillomavirus E7 ProteinsPDZ DomainsPhosphatidylinositol 3-KinasesPhosphorylationProtein BindingE6 protein, Human papillomavirus type 16oncogene protein E7, Human papillomavirus type 16Oncogene Proteins, ViralPapillomavirus E7 ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsRepressor ProteinsRNA, Small Interferingsodium-hydrogen exchanger regulatory factorSodium-Hydrogen Exchangers

Identifiers

PMID21680517
PMCPMC3147992
OpenAlexW2139807161

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.