Evidence map›Paper›PMID 18566754›Full record

ArticleMolecular and cellular biochemistry2008

CK2 mediates phosphorylation and ubiquitin-mediated degradation of the PML tumor suppressor.

P P Scaglioni, T M Yung, S Choi, S C Choi, C Baldini, G Konstantinidou, P P Pandolfi

Erratum issuedOpen access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Molecular and cellular biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-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

32 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
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  8. Article
  9. Synthesis of Novel Acyl Derivatives of 3-(4,5,6,7-Tetrabromo-1International journal of molecular sciences · 2021
    Article
  10. Targeting protein kinase CK2 in the treatment of cholangiocarcinoma.Exploration of targeted anti-tumor therapy · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
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  19. Article
  20. Differential Roles of PML Isoforms.Frontiers in oncology · 2013
    Article
4 · The record

Corrections and comments

  • Erratum issued
    Choi, S C [corrected to Choi, S]
5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

P P ScaglioniDivision of Hematology-Oncology, University of Texas Southwestern Medical Center, Dallas, TX 75390-8852, USA. pier.scaglioni@utsouthwestern.edu
T M Yung
S Choi
S C Choi
C Baldini
G Konstantinidou
P P Pandolfi
The University of Texas Southwestern Medical Center · USCancer Genetics (United States) · USMemorial Sloan Kettering Cancer Center · USSouthwestern Medical Center · US

Funding

PML, PLZF, NPM AND NUMA IN THE PATHOGENESIS OF APLR01CA071692 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI PANDOLFI, PIER PAOLO · 1996 to 2005
$1.8M
Post-transcriptional regulation of PML functionK08CA112325 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI SCAGLIONI, PIER PAOLO · 2005 to 2009
$669k
NCI NIH HHS K08 CA112325NCI NIH HHS R01 CA71692
6 · The paper itself

Abstract

The PML tumor suppressor controls growth suppression, induction of apoptosis, and cellular senescence. PML loss occurs frequently in hematopoietic and solid tumors. PML loss often correlates with tumor progression. Casein kinase 2 (CK2) is a stress-activated serine/threonine protein kinase that is oncogenic and frequently overexpressed in human tumor of multiple histological origins. In addition, CK2 overexpression due to gene amplification has been reported to be an adverse prognostic factor in non-small cell lung cancer. At the 5th International Conference on Protein Kinase CK2 in Padova, Italy, we reviewed our recent findings that PML undergoes ubiquitin/proteasome-mediated degradation in immortalized and tumor derived cell lines. PML degradation depends on direct CK2 phosphorylation of PML Ser517. PML mutants that are resistant to CK2 phosphorylation display increased tumor suppressive functions in assays measuring apoptosis, replicative senescence, and in xenograft models. More significantly, CK2 pharmacological inhibition enhances PML tumor suppressive property. These data identify a key post-translational mechanism that controls PML protein levels in cancer cells and suggest that CK2 inhibitors may be beneficial anti-cancer drugs.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCarcinoma, Non-Small-Cell LungCasein Kinase IICell Line, TumorEnzyme ActivationHumansLung NeoplasmsMiceMice, NudeMolecular Sequence DataMutationNuclear Proteinsp38 Mitogen-Activated Protein KinasesPhosphorylationCasein Kinase IINuclear Proteinsp38 Mitogen-Activated Protein KinasesPML protein, humanPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexProtein Kinase InhibitorsTranscription FactorsTumor Suppressor ProteinsUbiquitin

Identifiers

PMID18566754
OpenAlexW2112839337

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.