Evidence map›Paper›PMID 11485555›Full record

ArticleThe Biochemical journal2001

Assembly of protein kinase CK2: investigation of complex formation between catalytic and regulatory subunits using a zinc-finger-deficient mutant of CK2beta.

D A Canton, C Zhang, D W Litchfield

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

21 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Splicing Interruption by Intron Variants inFrontiers in neuroscience · 2022
    Article
  7. Predictive functional, statistical and structural analysis ofFrontiers in molecular biosciences · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. CK2 is a novel negative regulator of NADPH oxidase and a neuroprotectant in mice after cerebral ischemia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  16. Article
  17. B23 is a downstream target of polyamine-modulated CK2.Molecular and cellular biochemistry · 2005
    Article
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

D A CantonDepartment of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1, Canada.
C Zhang
D W Litchfield
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase CK2 is a tetrameric enzyme comprised of two regulatory subunits (CK2beta) and two catalytic subunits (CK2alpha and/or CK2alpha'). The crystal structure of dimeric CK2beta demonstrated that a zinc finger mediates CK2beta dimerization, therefore we constructed a mutant in which cysteine residues 109 and 114 were mutated to serine. Our objectives were to examine the effects of disrupting the zinc finger of the regulatory CK2beta subunit on CK2 tetramer assembly. Examination of this zinc-finger-deficient mutant of CK2beta using a yeast two-hybrid assay demonstrates that the mutant fails to form CK2beta homodimers. In order to extend these studies, we co-transfected COS-7 cells with epitope-tagged constructs and performed co-immunoprecipitation assays. The results from these studies demonstrate that the mutant fails to form CK2beta homodimers and fails to interact with catalytic CK2 subunits. Furthermore, we demonstrate that the mutant CK2beta is not appreciably phosphorylated in cells. Using in vitro binding assays, we demonstrated that the mutant CK2beta protein fails to interact with glutathione S-transferase-CK2alpha'. Finally, we demonstrate that the mutant is translated at an equivalent rate to wild-type CK2beta, but is degraded much more rapidly. Overall, our results are consistent with the model that beta-beta dimerization precedes incorporation of catalytic subunits into tetrameric CK2 complexes, and that beta-beta dimerization is a prerequisite for the stable incorporation of catalytic subunits into CK2 complexes.

Indexed as

MutationZinc FingersAnimalsbeta-GalactosidaseCasein Kinase IICatalysisCatalytic DomainCOS CellsDimerizationGlutathione TransferaseImmunoblottingPlasmidsPrecipitin TestsProtein BindingProtein BiosynthesisProtein Conformationbeta-GalactosidaseCasein Kinase IIGlutathione TransferaseProtein Serine-Threonine KinasesProtein Tyrosine PhosphatasesReceptor-Like Protein Tyrosine Phosphatases, Class 2Recombinant Fusion Proteins

Identifiers

PMID11485555
PMCPMC1222035
OpenAlexW2089087180

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.