Evidence map›Paper›PMID 22383878›Full record

ArticlePLoS pathogens2012

The invasive capacity of HPV transformed cells requires the hDlg-dependent enhancement of SGEF/RhoG activity.

Vanitha Krishna Subbaiah, Paola Massimi, Siaw Shi Boon, Michael P Myers, Lisa Sharek, Rafael Garcia-Mata, Lawrence Banks

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-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

28 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  5. Double inhibition and activation mechanisms of Ephexin family RhoGEFs.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

7 authors at 2 institutions in 2 countries.

Vanitha Krishna SubbaiahInternational Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Paola Massimi
Siaw Shi Boon
Michael P Myers
Lisa Sharek
Rafael Garcia-Mata
Lawrence Banks
International Centre for Genetic Engineering and Biotechnology · ITUniversity of North Carolina at Chapel Hill · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

A major target of the HPV E6 oncoprotein is the human Discs Large (hDlg) tumour suppressor, although how this interaction contributes to HPV-induced malignancy is still unclear. Using a proteomic approach we show that a strong interacting partner of hDlg is the RhoG-specific guanine nucleotide exchange factor SGEF. The interaction between hDlg1 and SGEF involves both PDZ and SH3 domain recognition, and directly contributes to the regulation of SGEF's cellular localization and activity. Consistent with this, hDlg is a strong enhancer of RhoG activity, which occurs in an SGEF-dependent manner. We also show that HPV-18 E6 can interact indirectly with SGEF in a manner that is dependent upon the presence of hDlg and PDZ binding capacity. In HPV transformed cells, E6 maintains a high level of RhoG activity, and this is dependent upon the presence of hDlg and SGEF, which are found in complex with E6. Furthermore, we show that E6, hDlg and SGEF each directly contributes to the invasive capacity of HPV-16 and HPV-18 transformed tumour cells. These studies demonstrate that hDlg has a distinct oncogenic function in the context of HPV induced malignancy, one of the outcomes of which is increased RhoG activity and increased invasive capacity.

Indexed as

Adaptor Proteins, Signal TransducingAlphapapillomavirusAnimalsCell AdhesionCell MovementCells, CulturedCell Transformation, ViralDiscs Large Homolog 1 ProteinGuanine Nucleotide Exchange FactorsHEK293 CellsHeLa CellsHuman papillomavirus 16Human papillomavirus 18HumansMembrane ProteinsMiceAdaptor Proteins, Signal TransducingARHGEF26 protein, humanDiscs Large Homolog 1 ProteinDLG1 protein, humanGuanine Nucleotide Exchange FactorsMembrane ProteinsRHOG protein, humanrho GTP-Binding Proteins

Identifiers

PMID22383878
PMCPMC3285591
OpenAlexW2085371447

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.