Evidence map›Paper›PMID 22553330›Full record

ArticleJournal of virology2012

Activation of cap-dependent translation by mucosal human papillomavirus E6 proteins is dependent on the integrity of the LXXLL binding motif.

Jennifer M Spangle, Nayana Ghosh-Choudhury, Karl Munger

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 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
2.3field-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

28 citing papers in PubMed, 32 citations in OpenAlex.

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  6. High-risk human papillomavirus-18 uses an mRNA sequence to synthesize oncoprotein E6 in tumors.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

3 authors at 2 institutions in 1 country.

Jennifer M SpangleDivision of Infectious Diseases, Brigham and Women's Hospital, Boston, MA, USA.
Nayana Ghosh-Choudhury
Karl Munger
Harvard University · USBrigham and Women's Hospital · US

Funding

MODULATION OF HOST CELL APOPTOTIC RESPONSES BY HPVE7R01CA081135 · NCI · TUFTS UNIVERSITY BOSTON · PI MUNGER, KARL · 2000 to 2014
$4.2M
VIRUS-HOST INTERACTIONS IN CANCERT32CA009031 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI KIEFF, ELLIOTT D · 1985 to 2009
$2.4M
NHLBI Short-Term Training Program to Increase Diversity in Health-Related ResearcR25HL089005 · NHLBI · HARVARD MEDICAL SCHOOL · PI MUNGER, KARL · 2007 to 2011
$484k
NCI NIH HHS R01 CA081135NCI NIH HHS R01CA081135NCI NIH HHS T32 CA009031NCI NIH HHS T32CA009031NHLBI NIH HHS R25 HL089005NHLBI NIH HHS R25 HL089005-01
6 · The paper itself

Abstract

The human papillomavirus (HPV) type 16 (HPV16) E6 protein can stimulate mechanistic target of rapamycin complex 1 (mTORC1) signaling and cap-dependent translation through activation of the PDK1 and mTORC2 kinases. Here we report that HPV18 E6 also enhances cap-dependent translation. The integrity of LXXLL and PDZ protein binding domains is important for activation of cap-dependent translation by high-risk mucosal HPV E6 proteins. Consistent with this model, low-risk mucosal HPV6b and HPV11 E6 proteins, which do not contain a PDZ protein binding motif, also activate cap-dependent translation and mTORC1, albeit at a lower efficiency than high-risk HPV E6 proteins. In contrast, cutaneous HPV5 and HPV8 E6 proteins, which lack LXXLL and PDZ motif protein binding, do not enhance cap-dependent translation. Mutagenic analyses of low-risk HPV E6 proteins revealed that association with the LXXLL motif containing ubiquitin ligase E6AP (UBE3A) correlates with activation of cap-dependent translation. Hence, activation of mTORC1 and cap-dependent translation may be important for the viral life cycle in specific epithelial tissue types and contribute to cellular transformation in cooperation with other biological activities of high-risk HPV E6-containing proteins.

Indexed as

PDZ DomainsProtein BiosynthesisProtein Interaction Domains and Motifs3-Phosphoinositide-Dependent Protein KinasesCell LineHEK293 CellsHuman papillomavirus 11Human papillomavirus 16Human papillomavirus 18HumansMechanistic Target of Rapamycin Complex 1Mucous MembraneMultiprotein ComplexesOncogene Proteins, ViralProteinsProtein Serine-Threonine Kinases3-Phosphoinositide-Dependent Protein KinasesCRTC2 protein, humanE6 protein, Human papillomavirus type 16Mechanistic Target of Rapamycin Complex 1Multiprotein ComplexesOncogene Proteins, ViralPDPK1 protein, humanProteinsProtein Serine-Threonine KinasesRepressor ProteinsTOR Serine-Threonine KinasesTranscription FactorsUBE3A protein, humanUbiquitin-Protein Ligases

Identifiers

PMID22553330
PMCPMC3416298
OpenAlexW2108564369

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.