Evidence map›Paper›PMID 9420248›Full record

ArticleJournal of virology1998

Interaction of the bovine papillomavirus E6 protein with the clathrin adaptor complex AP-1.

X Tong, W Boll, T Kirchhausen, P M Howley

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

20 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Review
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  6. Review
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  13. Article
  14. p600, a unique protein required for membrane morphogenesis and cell survival.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  15. Bovine papillomavirus E7 transformation function correlates with cellular p600 protein binding.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Papillomaviruses: a systematic review.Genetics and molecular biology
    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

4 authors at 2 institutions in 1 country.

X TongDepartment of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
W Boll
T Kirchhausen
P M Howley
Dana-Farber/Boston Children's Cancer and Blood Disorders Center · USHarvard University · US

Funding

VIRAL ONCOPROTEIN PERTURBATION OF RB/E2F PATHWAYP01CA050661 · NCI · DANA-FARBER CANCER INSTITUTE · PI HOWLEY, PETER M · 1989 to 2013
$35.8M
STRUCTURAL CHEMISTRY OF CLATHRIN &ASSOCIATED PROTEINSR01GM036548 · NIGMS · IMMUNE DISEASE INSTITUTE, INC. · PI KIRCHHAUSEN, TOMAS · 1986 to 2014
$9.8M
NCI NIH HHS P01 CA050661NCI NIH HHS P01CA50661-08NIGMS NIH HHS GM36548NIGMS NIH HHS R01 GM036548
6 · The paper itself

Abstract

The E6 gene of the bovine papillomavirus type 1 (BPV-1) is expressed in fibropapillomas caused by BPV-1 and in tissue culture cells transformed by BPV-1. It encodes one of the two major oncoproteins of BPV-1. In this study, we demonstrate an interaction between the BPV-1 E6 protein and AP-1, the TGN (trans-Golgi network)-specific clathrin adaptor complex. AP-1 is a four-subunit protein complex required for clathrin-mediated cellular transport from the TGN. The AP-1/E6 interaction was observed in vitro and in cells. The E6 binding site on AP-1 was mapped to the N-terminal trunk domain of the gamma subunit. BPV-1 E6 preferentially associated with membrane-bound AP-1 in cells but not with free cytosolic AP-1. BPV-1 E6 was further shown to be recruited to isolated Golgi membranes and to copurify with clathrin-coated vesicles. The recruitment of BPV-1 E6 to Golgi membranes was AP-1 independent, but the E6 interaction with AP-1 was required for its association with clathrin-coated vesicles. Furthermore, AP-1 proteins could compete with BPV-1 E6 for binding to Golgi membranes, suggesting that the recruitment of BPV-1 E6 and AP-1 to Golgi membranes involves a common factor. Taken together, our results suggest that cytosolic BPV-1 E6 is first recruited to the TGN, where it is then recognized by membrane-bound AP-1 and subsequently recruited into TGN-derived clathrin-coated vesicles. We propose that BPV-1 E6, through its interaction with AP-1, can affect cellular processes involving clathrin-mediated trafficking pathway.

Indexed as

Adaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesBovine papillomavirus 1CattleClathrinGenes, ViralGolgi ApparatusIn Vitro TechniquesMembrane ProteinsMembranesMolecular Sequence DataOncogene Proteins, ViralProtein BindingAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportClathrinMembrane ProteinsOncogene Proteins, Viralprotein E6, Bovine papillomavirusRecombinant Fusion Proteins

Identifiers

PMID9420248
PMCPMC109397
OpenAlexW2098766103

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.