Evidence map›Paper›PMID 15951851›Full record

ArticleInternational journal of biological sciences2005

The multiple personalities of the regulatory subunit of protein kinase CK2: CK2 dependent and CK2 independent roles reveal a secret identity for CK2beta.

Ashley C Bibby, David W Litchfield

Abstract read
In one paragraph

Article in International journal of biological sciences, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

101 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  5. Review
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  10. Review
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  12. CK2 Chemical Probes: Past, Present, and Future.Kinases and phosphatases · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Characterization of RAGE and CK2 Expressions in Human Fetal Membranes.International journal of molecular sciences · 2023
    Article
  18. Article
  19. Yeast Protein Asf1 Possesses Modulating Activity towards Protein Kinase CK2.International journal of molecular sciences · 2022
    Article
  20. Article

41 more citing papers are in PubMed but not listed here.

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

2 authors.

Ashley C BibbyDepartment of Biochemistry, Siebens-Drake Research Institute, University of Western Ontario, London, Ontario, Canada, N6A 5C1.
David W Litchfield

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase CK2 (formerly casein kinase II), an enzyme that participates in a wide variety of cellular processes, has traditionally been classified as a stable tetrameric complex consisting of two catalytic CK2alpha or CK2alpha' subunits and two regulatory CK2beta subunits. While consideration of CK2 as a tetrameric complex remains relevant, significant evidence has emerged to challenge the view that its individual subunits exist exclusively within these complexes. This review will summarize biochemical and genetic evidence indicating that the regulatory CK2beta subunit exists and performs functions independently of CK2 tetramers. For example, unbalanced expression of catalytic and regulatory CK2 subunits has been observed in a variety of tissues and tumors. Furthermore, localization studies including live cell imaging have demonstrated that while the catalytic and regulatory subunits of CK2 exhibit extensive co-localization, independent mobility of the individual CK2 subunits can also be observed within cells. Identification of proteins that interact with CK2beta in the absence of catalytic CK2 subunits reinforces the notion that CK2beta has functions distinct from CK2 and begins to offer insights into these CK2-independent functions. In this respect, the discovery that CK2beta can interact with and modulate the activity of a number of other serine/threonine protein kinases including A-Raf, c-Mos and Chk1 is particularly striking. This review will discuss the interactions between CK2beta and these protein kinases with special emphasis on the properties of CK2beta that mediate these interactions and on the implications of these interactions in yielding new prospects for elucidation of the cellular functions of CK2beta.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCasein Kinase IICell CompartmentationCell CycleEukaryotic CellsHumansMiceModels, MolecularMolecular Sequence DataPhosphorylationProtein BindingProtein ConformationProtein Interaction MappingProtein Processing, Post-TranslationalCasein Kinase IIProtein Serine-Threonine KinasesProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID15951851
PMCPMC1142214

What OpenQuestion holds

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Registered trials

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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.