Evidence map›Paper›PMID 24462519›Full record

ArticleMolecular oncology2014

Human papillomavirus (HPV)-18 E6 oncoprotein interferes with the epithelial cell polarity Par3 protein.

Florencia Facciuto, Marina Bugnon Valdano, Federico Marziali, Paola Massimi, Lawrence Banks, Ana Laura Cavatorta, Daniela Gardiol

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular oncology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

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  11. PDZ Domains as Drug Targets.Advanced therapeutics · 2019
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Florencia FacciutoInstituto de Biología Molecular y Celular de Rosario-CONICET, Area Virología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Suipacha 531, Universidad Nacional de Rosario, Rosario, Argentina.
Marina Bugnon ValdanoInstituto de Biología Molecular y Celular de Rosario-CONICET, Area Virología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Suipacha 531, Universidad Nacional de Rosario, Rosario, Argentina.
Federico MarzialiInstituto de Biología Molecular y Celular de Rosario-CONICET, Area Virología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Suipacha 531, Universidad Nacional de Rosario, Rosario, Argentina.
Paola MassimiInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste, Italy.
Lawrence BanksInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste, Italy.
Ana Laura CavatortaInstituto de Biología Molecular y Celular de Rosario-CONICET, Area Virología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Suipacha 531, Universidad Nacional de Rosario, Rosario, Argentina.
Daniela GardiolInstituto de Biología Molecular y Celular de Rosario-CONICET, Area Virología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Suipacha 531, Universidad Nacional de Rosario, Rosario, Argentina. Electronic address: gardiol@ibr-conicet.gov.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARInternational Centre for Genetic Engineering and Biotechnology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-risk human papillomavirus (HPV) infection is the principal risk factor for the development of cervical cancer. The HPV E6 oncoprotein has the ability to target and interfere with several PSD-95/DLG/ZO-1 (PDZ) domain-containing proteins that are involved in the control of cell polarity. This function can be significant for E6 oncogenic activity because a deficiency in cell polarisation is a marker of tumour progression. The establishment and control of polarity in epithelial cells depend on the correct asymmetrical distribution of proteins and lipids at the cell borders and on specialised cell junctions. In this report, we have investigated the effects of HPV E6 protein on the polarity machinery, with a focus on the PDZ partitioning defective 3 (Par3) protein, which is a key component of tight junctions (TJ) and the polarity network. We demonstrate that E6 is able to bind and induce the mislocalisation of Par3 protein in a PDZ-dependent manner without significant reduction in Par3 protein levels. In addition, the high-risk HPV-18 E6 protein promotes a delay in TJ formation when analysed by calcium switch assays. Taken together, the data presented in this study contribute to our understanding of the molecular mechanism by which HPVs induce the loss of cell polarity, with potential implications for the development and progression of HPV-associated tumours.

Indexed as

Cell PolarityHost-Pathogen InteractionsAdaptor Proteins, Signal TransducingCell Cycle ProteinsCell LineDNA-Binding ProteinsEpithelial CellsHuman papillomavirus 18HumansMembrane ProteinsOncogene Proteins, ViralPapillomavirus InfectionsProteasome Endopeptidase ComplexProtein BindingTight JunctionsAdaptor Proteins, Signal TransducingCell Cycle ProteinsDNA-Binding ProteinsE6 protein, Human papillomavirus type 18Membrane ProteinsOncogene Proteins, ViralPARD3 protein, humanProteasome Endopeptidase ComplexCell polarityE6 proteinHPVPar3PDZ

Identifiers

PMID24462519
PMCPMC5528639
OpenAlexW2006747001

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.