Evidence map›Paper›PMID 18621739›Full record

ArticleThe Journal of biological chemistry2008

Acetylation of PML is involved in histone deacetylase inhibitor-mediated apoptosis.

Fumihiko Hayakawa, Akihiro Abe, Issay Kitabayashi, Pier Paolo Pandolfi, Tomoki Naoe

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. PML::RARA and GATA2 proteins interact via DNA templates to induce aberrant self-renewal in mouse and human hematopoietic cells.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. The PML hub: An emerging actor of leukemia therapies.The Journal of experimental medicine · 2023
    Article
  4. Article
  5. Review
  6. Review
  7. Article
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  10. Review
  11. Review
  12. Article
  13. Article
  14. PML: Not all about Tumor Suppression.Frontiers in oncology · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The nuclear bodies inside out: PML conquers the cytoplasm.Current opinion in cell biology · 2011
    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

5 authors at 3 institutions in 3 countries.

Fumihiko HayakawaDepartment of Hematology and Oncology, Nagoya University, Graduate School of Medicine, Nagoya 466-8550, Japan. bun-hy@med.nagoya-u.ac.jp
Akihiro Abe
Issay Kitabayashi
Pier Paolo Pandolfi
Tomoki Naoe
Nagoya University · JPBeth Israel Deaconess Medical Center · USNational Cancer Research Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PML is a potent tumor suppressor and proapoptotic factor and is functionally regulated by post-translational modifications such as phosphorylation, sumoylation, and ubiquitination. Histone deacetylase (HDAC) inhibitors are a promising class of targeted anticancer agents and induce apoptosis in cancer cells by largely unknown mechanisms. We report here a novel post-transcriptional modification, acetylation, of PML. PML exists as an acetylated protein in HeLa cells, and its acetylation is enhanced by coexpression of p300 or treatment with a HDAC inhibitor, trichostatin A. Increased PML acetylation is associated with increased sumoylation of PML in vitro and in vivo. PML is involved in trichostatin A-induced apoptosis and PML with an acetylation-defective mutation shows an inability to mediate apoptosis, suggesting the importance of PML acetylation. Our work provides new insights into PML regulation by post-translational modification and new information about the therapeutic mechanism of HDAC inhibitors.

Indexed as

Histone Deacetylase InhibitorsAcetylationAnimalsApoptosisApoptosis Regulatory ProteinsEnzyme InhibitorsHeLa CellsHistone DeacetylasesHumansHydroxamic AcidsMiceMutationNuclear ProteinsPhosphorylationPromyelocytic Leukemia ProteinProtein Processing, Post-TranslationalApoptosis Regulatory ProteinsEnzyme InhibitorsHistone Deacetylase InhibitorsHistone DeacetylasesHydroxamic AcidsNuclear ProteinsPML protein, humanPml protein, mousePromyelocytic Leukemia ProteinTranscription Factorstrichostatin ATumor Suppressor Proteins

Identifiers

PMID18621739
PMCPMC3259823
OpenAlexW2052440970

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.