Evidence map›Paper›PMID 21228238›Full record

ArticleJournal of virology2011

Polyomavirus middle T-antigen is a transmembrane protein that binds signaling proteins in discrete subcellular membrane sites.

Alice Y Zhou, Natalia Ichaso, Adam Adamarek, Vojtech Zila, Jitka Forstova, Nicholas J Dibb, Stephen M Dilworth

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
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  4. Membrane-bound Merkel cell polyomavirus middle T protein constitutively activates PLCγ1 signaling through Src-family kinases.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  5. Article
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  13. Identification of an overprinting gene in Merkel cell polyomavirus provides evolutionary insight into the birth of viral genes.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Review
  15. 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

7 authors at 3 institutions in 2 countries.

Alice Y ZhouCell Transformation Group, Section of Investigative Medicine, IRDB Building, Imperial College London, Hammersmith Hospital Campus, Du Cane Road, London W12 0NN, United Kingdom.
Natalia Ichaso
Adam Adamarek
Vojtech Zila
Jitka Forstova
Nicholas J Dibb
Stephen M Dilworth
Hammersmith Hospital · GBCharles University · CZImperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/B/06962Biotechnology and Biological Sciences Research Council C19979
6 · The paper itself

Abstract

Murine polyomavirus middle T-antigen (MT) induces tumors by mimicking an activated growth factor receptor. An essential component of this action is a 22-amino-acid hydrophobic region close to the C terminus which locates MT to cell membranes. Here, we demonstrate that this sequence is a transmembrane domain (TMD) by showing that a hemagglutinin (HA) tag added to the MT C terminus is exposed on the outside of the cells, with the N terminus inside. To determine whether this MT TMD is inserted into the endoplasmic reticulum (ER) membrane, we added the ER retention signal KDEL to the MT C terminus (MTKDEL). This mutant protein locates only in the ER, demonstrating that MT does insert into membranes solely at this location. In addition, this ER-located MT failed to transform. Examination of the binding proteins associated with the MTKDEL protein demonstrated that it associates with PP2A and c-Src but fails to interact with ShcA, phosphatidylinositol 3-kinase (PI3K), and phospholipase C-γ1 (PLC-γ1), despite being tyrosine phosphorylated. Additional mutant and antibody studies show that MT binding to PP2A is probably required for MT to efficiently exit the ER and migrate to the plasma membrane though the TMD also plays a role in this relocation. Overall, these data, together with previous publications, illustrate that MT associates with signaling proteins at different sites in its maturation pathway. MT binds to PP2A in the cytoplasm, to c-Src at the endoplasmic reticulum, and to ShcA, PI3K, and PLC-γ1 at subsequent locations en route to the plasma membrane.

Indexed as

Signal TransductionAnimalsAntigens, Viral, TumorCell LineCell MembraneCSK Tyrosine-Protein KinaseEndoplasmic ReticulumMembrane ProteinsMicePhosphatidylinositol 3-KinasesPhospholipase C gammaPolyomavirusProtein BindingProtein Phosphatase 2Protein Sorting SignalsProtein Structure, TertiaryAntigens, Viral, TumorCSK Tyrosine-Protein KinaseMembrane ProteinsPhosphatidylinositol 3-KinasesPhospholipase C gammaProtein Phosphatase 2Protein Sorting SignalsProtein-Tyrosine KinasesShc1 protein, ratShc Signaling Adaptor Proteinssrc-Family KinasesSrc Homology 2 Domain-Containing, Transforming Protein 1

Identifiers

PMID21228238
PMCPMC3067864
OpenAlexW2116347395

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.