Evidence map›Paper›PMID 16840333›Full record

ArticleJournal of virology2006

Apoptin nucleocytoplasmic shuttling is required for cell type-specific localization, apoptosis, and recruitment of the anaphase-promoting complex/cyclosome to PML bodies.

Destin W Heilman, Jose G Teodoro, Michael R Green

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. Gyrovirus: current status and challenge.Frontiers in microbiology · 2024
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The Role of Apoptin in Chicken Anemia Virus Replication.Pathogens (Basel, Switzerland) · 2020
    Review
  12. Article
  13. Apoptosis Triggered by ORF3 Proteins of theFrontiers in cellular and infection microbiology · 2020
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
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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.

Destin W HeilmanHoward Hughes Medical Institute, and Program in Gene Function and Expression, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA 01605, USA.
Jose G Teodoro
Michael R Green
Howard Hughes Medical Institute · USUniversity of Massachusetts Chan Medical School · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chicken anemia virus protein Apoptin selectively induces apoptosis in transformed cells while leaving normal cells intact. This selectivity is thought to be largely due to cell type-specific localization: Apoptin is cytoplasmic in primary cells and nuclear in transformed cells. The basis of Apoptin cell type-specific localization and activity remains to be determined. Here we show that Apoptin is a nucleocytoplasmic shuttling protein whose localization is mediated by an N-terminal nuclear export signal (NES) and a C-terminal nuclear localization signal (NLS). Both signals are required for cell type-specific localization, since Apoptin fragments containing either the NES or the NLS fail to differentially localize in transformed and primary cells. Significantly, cell type-specific localization can be conferred in trans by coexpression of the two separate fragments, which interact through an Apoptin multimerization domain. We have previously shown that Apoptin interacts with the APC1 subunit of the anaphase-promoting complex/cyclosome (APC/C), resulting in G(2)/M cell cycle arrest and apoptosis in transformed cells. We found that the nucleocytoplasmic shuttling activity is critical for efficient APC1 association and induction of apoptosis in transformed cells. Interestingly, both Apoptin multimerization and APC1 interaction are mediated by domains that overlap with the NES and NLS sequences, respectively. Apoptin expression in transformed cells induces the formation of PML nuclear bodies and recruits APC/C to these subnuclear structures. Our results reveal a mechanism for the selective killing of transformed cells by Apoptin.

Indexed as

Active Transport, Cell NucleusApoptosisAnaphase-Promoting Complex-CyclosomeApc1 Subunit, Anaphase-Promoting Complex-CyclosomeCapsid ProteinsCarcinoma, Non-Small-Cell LungCell Line, TransformedCell NucleusChicken anemia virusCytoplasmFibroblastsHumansIntranuclear Inclusion BodiesLung NeoplasmsMicroscopy, FluorescenceNuclear Export SignalsANAPC1 protein, humanAnaphase-Promoting Complex-CyclosomeApc1 Subunit, Anaphase-Promoting Complex-CyclosomeCapsid ProteinsNuclear Export SignalsNuclear Localization SignalsUbiquitin-Protein Ligase ComplexesVP3 protein, Chicken anemia virus

Identifiers

PMID16840333
PMCPMC1563728
OpenAlexW2127892739

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.