Evidence map›Paper›PMID 22773875›Full record

ArticleThe Journal of biological chemistry2012

Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation.

Yunyun Geng, Shamci Monajembashi, Anwen Shao, Di Cui, Weiyong He, Zhongzhou Chen, Peter Hemmerich, Jun Tang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Discovery of novel murine PML isoforms.Nucleus (Austin, Tex.) · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. PML Body Biogenesis: A Delicate Balance of Interactions.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. [Involvement of PML proteins in treatment of acute promyelocytic leukemia with arsenic trioxide].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2018
    Review
  14. Article
  15. Review
  16. Article
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  20. Review
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

8 authors at 4 institutions in 3 countries.

Yunyun GengState Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
Shamci Monajembashi
Anwen Shao
Di Cui
Weiyong He
Zhongzhou Chen
Peter Hemmerich
Jun Tang
China Agricultural University · CNAgrobiotechnology Institute · ESLeibniz Association · DELeibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Promyelocytic leukemia protein (PML) nuclear bodies are dynamic and heterogeneous nuclear protein complexes implicated in various important functions, most notably tumor suppression. PML is the structural component of PML nuclear bodies and has several nuclear splice isoforms that share a common N-terminal region but differ in their C termini. Previous studies have suggested that the coiled-coil motif within the N-terminal region is sufficient for PML nuclear body formation by mediating homo/multi-dimerization of PML molecules. However, it has not been investigated whether any of the C-terminal variants of PML may contribute to PML body assembly. Here we report that the unique C-terminal domains of PML-II and PML-V can target to PML-NBs independent of their N-terminal region. Strikingly, both domains can form nuclear bodies in the absence of endogenous PML. The C-terminal domain of PML-II interacts transiently with unknown binding sites at PML nuclear bodies, whereas the C-terminal domain of PML-V exhibits hyperstable binding to PML bodies via homo-dimerization. This strong interaction is mediated by a putative α-helix in the C terminus of PML-V. Moreover, nuclear bodies assembled from the C-terminal domain of PML-V also recruit additional PML body components, including Daxx and Sp100. These observations establish the C-terminal domain of PML-V as an additional important contributor to the assembly mechanism(s) of PML bodies.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsAntigens, NuclearAutoantigensCarrier ProteinsCo-Repressor ProteinsHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsIntranuclear Inclusion BodiesMiceMice, KnockoutMolecular ChaperonesNuclear ProteinsPromyelocytic Leukemia ProteinAdaptor Proteins, Signal TransducingAntigens, NuclearAutoantigensCarrier ProteinsCo-Repressor ProteinsDAXX protein, humanDaxx protein, mouseIntracellular Signaling Peptides and ProteinsMolecular ChaperonesNuclear ProteinsPML protein, humanPml protein, mousePromyelocytic Leukemia ProteinProtein IsoformsSP100 protein, humanSp100 protein, mouseTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID22773875
PMCPMC3436317
OpenAlexW2060552146

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.