Evidence map›Paper›PMID 29346075›Full record

ArticleVirology2018

Human Papillomavirus E6 interaction with cellular PDZ domain proteins modulates YAP nuclear localization.

Sydney Webb Strickland, Nicole Brimer, Charles Lyons, Scott B Vande Pol

Open access · greenAbstract read
In one paragraph

Article in Virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

31 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Microbiology spectrum · 2023
    Article
  12. Article
  13. Frontiers in cellular and infection microbiology · 2023
    Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. HTLV-1 activates YAP via NF-κB/p65 to promote oncogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

4 authors at 1 institution in 1 country.

Sydney Webb StricklandDepartment of Pathology, University of Virginia, Charlottesville, VA 22901, United States.
Nicole BrimerDepartment of Pathology, University of Virginia, Charlottesville, VA 22901, United States.
Charles LyonsDepartment of Pathology, University of Virginia, Charlottesville, VA 22901, United States.
Scott B Vande PolDepartment of Pathology, University of Virginia, Charlottesville, VA 22901, United States. Electronic address: vandepol@virginia.edu.
University of Virginia · US

Funding

Cancer Research Training Program: From Molecular Mechanisms to Therapeutic StrategiesT32CA009109 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Andrew Carl Dudley, Melanie R Rutkowski · 1985 to 2026
$13.9M
Papillomavirus E6 Structural ConsortiumR01CA134737 · NCI · UNIVERSITY OF VIRGINIA · PI VANDE POL, SCOTT BRIAN · 2010 to 2019
$4.2M
E6 Interaction with Cellular PDZ ProteinsR01CA120352 · NCI · UNIVERSITY OF VIRGINIA · PI VANDE POL, SCOTT BRIAN · 2007 to 2010
$1.2M
NCI NIH HHS R01 CA120352NCI NIH HHS R01 CA134737NCI NIH HHS T32 CA009109
6 · The paper itself

Abstract

HPV E6 oncoproteins associate with cellular PDZ proteins. In addition to previously identified cellular PDZ proteins, we found association of the HPV16 E6 PBM with the Dystrophin Glycoprotein Complex, LRCC1, and SLC9A3R2. HPV18 E6 had additional associations when lysates from adenomatous cell lines were used including LRPPRC, RLGAPB, EIF3A, SMC2 and 3, AMOT, AMOTL1, and ARHGEF1; some of these cellular PDZ proteins are implicated in the regulation of the YAP1 transcriptional co-activator. In keratinocytes, nuclear translocation of YAP1 was promoted by the complete HPV-16 genome, or by expression of the individual E6 or E7 oncoproteins; the activity of E6 required an intact PBM at the carboxy-terminus. This work demonstrates that E6 association with cellular PDZ proteins promotes the nuclear localization of YAP1. The ability of E6 to promote the nuclear transport of YAP1 thus identifies an E6 activity that could contribute to the transformation of cells by E6.

Indexed as

Adaptor Proteins, Signal TransducingCell NucleusDNA-Binding ProteinsHuman papillomavirus 16Human papillomavirus 18HumansOncogene Proteins, ViralPapillomavirus E7 ProteinsPapillomavirus InfectionsPDZ DomainsPhosphoproteinsProtein BindingProtein TransportRepressor ProteinsTranscription FactorsYAP-Signaling ProteinsAdaptor Proteins, Signal TransducingDNA-Binding ProteinsE6 protein, Human papillomavirus type 16E6 protein, Human papillomavirus type 18Oncogene Proteins, ViralPapillomavirus E7 ProteinsPhosphoproteinsRepressor ProteinsTranscription FactorsYAP1 protein, humanYAP-Signaling ProteinsAdherens junctionsHippoPolarityTAZTight junctions

Identifiers

PMID29346075
PMCPMC5826896
OpenAlexW2783354257

What OpenQuestion holds

Textmetadata
LicenceTDM
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.