Evidence map›Paper›PMID 12032843›Full record

ArticleOncogene2002

Phosphorylation regulates the stability of the regulatory CK2beta subunit.

Cunjie Zhang, Greg Vilk, David A Canton, David W Litchfield

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.7field-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

39 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
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  9. Article
  10. Predictive functional, statistical and structural analysis ofFrontiers in molecular biosciences · 2022
    Article
  11. Review
  12. Synthesis of Novel Acyl Derivatives of 3-(4,5,6,7-Tetrabromo-1International journal of molecular sciences · 2021
    Article
  13. Article
  14. Protein Kinase CK2, a Potential Therapeutic Target in Carcinoma ManagementAsian Pacific journal of cancer prevention : APJCP · 2019
    Review
  15. Article
  16. Review
  17. Review
  18. Article
  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.

Cunjie ZhangDepartment of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.
Greg Vilk
David A Canton
David W Litchfield
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase CK2 is a protein serine/threonine kinase that exhibits elevated expression in a number of cancers and displays oncogenic activity in mice. The regulatory CK2beta subunit has a central role in assembly of functional tetrameric CK2 complexes where it participates in modulation of catalytic activity and substrate specificity. Since overexpression of CK2beta results in elevated levels of CK2 activity, we investigated the molecular mechanisms that control its degradation since perturbations in these pathways could contribute to elevated CK2 in cancer. In this study, we demonstrate that CK2beta is degraded by a proteasome-dependent pathway and that it is ubiquitinated. We have also investigated the role of phosphorylation and a putative destruction box in regulating its stability in cells. Importantly, replacement of three serine residues within the autophosphorylation site of CK2beta with glutamic acid residues resulted in a significant decrease in its degradation indicating that autophosphorylation is involved in regulating its stability. Notably, although the autophosphorylation site of CK2beta is remarkably conserved between species, this is the first functional role ascribed to this site. Furthermore, based on these results, we speculate that alterations in the phosphorylation or dephosphorylation of the regulatory CK2beta subunit could underlie the elevated expression of CK2 that is observed in cancer cells.

Indexed as

AnimalsCasein Kinase IIChickensCOS CellsCysteine EndopeptidasesEnzyme InhibitorsEnzyme StabilityHumansMultienzyme ComplexesMutationPhosphorylationProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesProtein SubunitsTumor Cells, CulturedUbiquitinsCasein Kinase IICysteine EndopeptidasesEnzyme InhibitorsMultienzyme ComplexesProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesProtein SubunitsUbiquitins

Identifiers

PMID12032843
OpenAlexW2314221598

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.