Nuclear import of cutaneous beta genus HPV8 E7 oncoprotein is mediated by hydrophobic interactions between its zinc-binding domain and FG nucleoporins.

Zeynep Onder, Junona Moroianu

Abstract read

In one paragraph

Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it

0cells of the map it votes in

4citing papers in PubMed

0.4field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

Strategies for the Viral Exploitation of Nuclear Pore Transport Pathways.Viruses · 2025
Review
How SARS-CoV-2 and Other Viruses Build an Invasion Route to Hijack the Host Nucleocytoplasmic Trafficking System.Cells · 2021
Review
Active Targeting of the Nucleus Using Nonpeptidic Boronate Tags.Journal of the American Chemical Society · 2017
Article
Nuclear export of cutaneous HPV8 E7 oncoprotein is mediated by a leucine-rich nuclear export signal via a CRM1 pathway.Virology · 2015
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

2 authors at 1 institution in 1 country.

Zeynep OnderBiology Department, Boston College, Chestnut Hill, MA 02467, USA.

Junona MoroianuBiology Department, Boston College, Chestnut Hill, MA 02467, USA. Electronic address: moroianu@bc.edu.

Boston College · US

Funding

Nuclear Import Pathways for HPV MacromoleculesR01CA094898 · NCI · BOSTON COLLEGE · PI MOROIANU, JUNONA F · 2002 to 2010

$2.0M

NCI NIH HHS R01 CA094898NCI NIH HHS R01CA94898

6 · The paper itself

Abstract

We have previously discovered and characterized the nuclear import pathways for the E7 oncoproteins of mucosal alpha genus HPVs, type 16 and 11. Here we investigated the nuclear import of cutaneous beta genus HPV8 E7 protein using confocal microscopy after transfections of HeLa cells with EGFP-8E7 and mutant plasmids and nuclear import assays in digitonin-permeabilized HeLa cells. We determined that HPV8 E7 contains a nuclear localization signal (NLS) within its zinc-binding domain that mediates its nuclear import. Furthermore, we discovered that a mostly hydrophobic patch 65LRLFV69 within the zinc-binding domain is essential for the nuclear import and localization of HPV8 E7 via hydrophobic interactions with the FG nucleoporins Nup62 and Nup153. Substitution of the hydrophobic residues within the 65LRLFV69 patch to alanines, and not R66A mutation, disrupt the interactions between the 8E7 zinc-binding domain and Nup62 and Nup153 and consequently inhibit nuclear import of HPV8 E7.

Indexed as

Active Transport, Cell NucleusBetapapillomavirusCell NucleusHumansHydrophobic and Hydrophilic InteractionsMembrane GlycoproteinsNuclear Localization SignalsNuclear Pore Complex ProteinsPapillomavirus E7 ProteinsPapillomavirus InfectionsProtein BindingProtein Structure, TertiaryZinc FingersMembrane GlycoproteinsNuclear Localization SignalsNuclear Pore Complex Proteinsnuclear pore protein p62NUP153 protein, humanPapillomavirus E7 ProteinsBeta genus human papillomavirusesEGFPenhanced green fluorescent proteinFG nucleoporinsglutathione-S-transferaseGSTHPVHPV8 E7 oncoproteinhuman papillomavirusNESNLSNPCnuclear export signalnuclear localization signalNuclear localization signalnuclear pore complexNup153Nup62

Identifiers

PMID24418548

DOI10.1016/j.virol.2013.11.020

PMCPMC3894589

OpenAlexW2093389851

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Registered trials

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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.