Evidence map›Paper›PMID 19509278›Full record

ArticleThe Journal of biological chemistry2009

Differential phosphorylation of plant translation initiation factors by Arabidopsis thaliana CK2 holoenzymes.

Michael D Dennis, Karen S Browning

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Rapid COThe Plant journal : for cell and molecular biology · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Crystal structure of Arabidopsis thaliana casein kinase 2 α1.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  9. What makes ribosomes tick?RNA biology · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Mechanism of cytoplasmic mRNA translation.The arabidopsis book · 2015
    Article
  17. Article
  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

2 authors.

Michael D DennisDepartment of Chemistry and Biochemistry and the Institute for Cellular and Molecular Biology, University of Texas, Austin, Texas 78712, USA.
Karen S Browning

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A previously described wheat germ protein kinase (Yan, T. F., and Tao, M. (1982) J. Biol. Chem. 257, 7037-7043) was identified unambiguously as CK2 using mass spectrometry. CK2 is a ubiquitous eukaryotic protein kinase that phosphorylates a wide range of substrates. In previous studies, this wheat germ kinase was shown to phosphorylate eIF2alpha, eIF3c, and three large subunit (60 S) ribosomal proteins (Browning, K. S., Yan, T. F., Lauer, S. J., Aquino, L. A., Tao, M., and Ravel, J. M. (1985) Plant Physiol. 77, 370-373). To further characterize the role of CK2 in the regulation of translation initiation, Arabidopsis thaliana catalytic (alpha1 and alpha2) and regulatory (beta1, beta2, beta3, and beta4) subunits of CK2 were cloned and expressed in Escherichia coli. Recombinant A. thaliana CK2beta subunits spontaneously dimerize and assemble into holoenzymes in the presence of either CK2alpha1 or CK2alpha2 and exhibit autophosphorylation. The purified CK2 subunits were used to characterize the properties of the individual subunits and their ability to phosphorylate various plant protein substrates. CK2 was shown to phosphorylate eIF2alpha, eIF2beta, eIF3c, eIF4B, eIF5, and histone deacetylase 2B but did not phosphorylate eIF1, eIF1A, eIF4A, eIF4E, eIF4G, eIFiso4E, or eIFiso4G. Differential phosphorylation was exhibited by CK2 in the presence of various regulatory beta-subunits. Analysis of A. thaliana mutants either lacking or overexpressing CK2 subunits showed that the amount of eIF2beta protein present in extracts was affected, which suggests that CK2 phosphorylation may play a role in eIF2beta stability. These results provide evidence for a potential mechanism through which the expression and/or subcellular distribution of CK2 beta-subunits could participate in the regulation of the initiation of translation and other physiological processes in plants.

Indexed as

ArabidopsisBiocatalysisCasein Kinase IIChromatography, GelComputational BiologyElectrophoresis, Polyacrylamide GelHoloenzymesPeptide Initiation FactorsPhosphorylationPlants, Genetically ModifiedProtein KinasesProtein StabilityProtein Structure, QuaternaryProtein SubunitsRecombinant ProteinsSubstrate SpecificityCasein Kinase IIHoloenzymesPeptide Initiation FactorsProtein KinasesProtein SubunitsRecombinant Proteins

Identifiers

PMID19509278
PMCPMC2742825

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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.