Evidence map›Paper›PMID 20943951›Full record

ArticleMolecular biology of the cell2010

Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies.

Marie-Claude Geoffroy, Ellis G Jaffray, Katherine J Walker, Ronald T Hay

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

55 citing papers in PubMed, 98 citations in OpenAlex.

  1. Discovery of novel murine PML isoforms.Nucleus (Austin, Tex.) · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Nuclear p62 condensates stabilize the promyelocytic leukemia nuclear bodies by sequestering their ubiquitin ligase RNF4.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. SUMO control of centromere homeostasis.Frontiers in cell and developmental biology · 2023
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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 1 institution in 1 country.

Marie-Claude GeoffroyWellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD15EH, UK.
Ellis G Jaffray
Katherine J Walker
Ronald T Hay
University of Dundee · GB

Funding

Cancer Research UKWellcome Trust
6 · The paper itself

Abstract

In acute promyelocytic leukemia (APL), the promyelocytic leukemia (PML) protein is fused to the retinoic acid receptor alpha (RAR). Arsenic is an effective treatment for this disease as it induces SUMO-dependent ubiquitin-mediated proteasomal degradation of the PML-RAR fusion protein. Here we analyze the nuclear trafficking dynamics of PML and its SUMO-dependent ubiquitin E3 ligase, RNF4 in response to arsenic. After administration of arsenic, PML immediately transits into nuclear bodies where it undergoes SUMO modification. This initial recruitment of PML into nuclear bodies is not dependent on RNF4, but RNF4 quickly follows PML into the nuclear bodies where it is responsible for ubiquitylation of SUMO-modified PML and its degradation by the proteasome. While arsenic restricts the mobility of PML, FRAP analysis indicates that RNF4 continues to rapidly shuttle into PML nuclear bodies in a SUMO-dependent manner. Under these conditions FRET studies indicate that RNF4 interacts with SUMO in PML bodies but not directly with PML. These studies indicate that arsenic induces the rapid reorganization of the cell nucleus by SUMO modification of nuclear body-associated PML and uptake of the ubiquitin E3 ligase RNF4 leading to the ubiquitin-mediated degradation of PML.

Indexed as

ArsenicBlotting, WesternFluorescent Antibody TechniqueHeLa CellsHumansImmunoprecipitationNuclear ProteinsOncogene Proteins, FusionPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexReceptors, Retinoic AcidReverse Transcriptase Polymerase Chain ReactionSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsTumor Suppressor ProteinsUbiquitinArsenicNuclear ProteinsOncogene Proteins, FusionPML protein, humanPromyelocytic Leukemia Proteinpromyelocytic leukemia-retinoic acid receptor alpha fusion oncoproteinProteasome Endopeptidase ComplexReceptors, Retinoic AcidRNF4 protein, humanSmall Ubiquitin-Related Modifier ProteinsTranscription FactorsTumor Suppressor ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID20943951
PMCPMC2993750
OpenAlexW2125848058

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.