Evidence map›Paper›PMID 17166906›Full record

ArticleJournal of virology2007

Degradation of tyrosine phosphatase PTPN3 (PTPH1) by association with oncogenic human papillomavirus E6 proteins.

Ming Jing, Joanna Bohl, Nicole Brimer, Michael Kinter, Scott B Vande Pol

Abstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

51 citing papers in PubMed, 106 citations in OpenAlex.

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  16. Regulating the human HECT E3 ligases.Cellular and molecular life sciences : CMLS · 2018
    Review
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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

5 authors at 3 institutions in 1 country.

Ming JingDepartment of Pathology, University of Virginia, P.O. Box 800904, Charlottesville, VA 22908, USA.
Joanna Bohl
Nicole Brimer
Michael Kinter
Scott B Vande Pol
Case Western Reserve University · USUniversity of Virginia · USCleveland Clinic · US

Funding

Papillomavirus TransformationR01CA069292 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI VANDE POL, SCOTT BRIAN · 2002 to 2006
$1.4M
STRUCTURAL FEATURES OF PAPILLOMAVIRUS E6 ONCOPROTEINSR01CA080931 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI VANDE POL, SCOTT BRIAN · 2000 to 2004
$1.3M
PAPILLOMAVIRUS TRANSFORMATIONR29CA069292 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI VANDE POL, SCOTT B · 1996 to 2000
$35k
NCI NIH HHS CA 69292NCI NIH HHS CA 80931NCI NIH HHS R01 CA069292NCI NIH HHS R01 CA080931NCI NIH HHS R29 CA069292
6 · The paper itself

Abstract

Oncoproteins from DNA tumor viruses associate with critical cellular proteins to regulate cell proliferation, survival, and differentiation. Human papillomavirus (HPV) E6 oncoproteins have been previously shown to associate with a cellular HECT domain ubiquitin ligase termed E6AP (UBE3A). Here we show that the E6-E6AP complex associates with and targets the degradation of the protein tyrosine phosphatase PTPN3 (PTPH1) in vitro and in living cells. PTPN3 is a membrane-associated tyrosine phosphatase with FERM, PDZ, and PTP domains previously implicated in regulating tyrosine phosphorylation of growth factor receptors and p97 VCP (valosin-containing protein, termed Cdc48 in Saccharomyces cerevisiae) and is mutated in a subset of colon cancers. Degradation of PTPN3 by E6 requires E6AP, the proteasome, and an interaction between the carboxy terminus of E6 and the PDZ domain of PTPN3. In transduced keratinocytes, E6 confers reduced growth factor requirements, a function that requires the PDZ ligand of E6 and that can in part be replicated by inhibiting the expression of PTPN3. This report demonstrates the potential of E6 to regulate phosphotyrosine metabolism through the targeted degradation of a tyrosine phosphatase.

Indexed as

Amino Acid SequenceBase SequenceBinding SitesCell LineDNAHuman papillomavirus 16HumansIn Vitro TechniquesLigandsMolecular Sequence DataMultiprotein ComplexesOncogene Proteins, ViralProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 3Protein Tyrosine PhosphatasesRecombinant ProteinsDNAE6 protein, Human papillomavirus type 16LigandsMultiprotein ComplexesOncogene Proteins, ViralProtein Tyrosine Phosphatase, Non-Receptor Type 3Protein Tyrosine PhosphatasesPTPN3 protein, humanRecombinant ProteinsRepressor ProteinsUBE3A protein, humanUbiquitin-Protein Ligases

Identifiers

PMID17166906
PMCPMC1865939
OpenAlexW2171213086

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.