Evidence map›Paper›PMID 12628006›Full record

ArticleThe Biochemical journal2003

Tyrosine phosphorylation of protein kinase CK2 by Src-related tyrosine kinases correlates with increased catalytic activity.

Arianna Donella-Deana, Luca Cesaro, Stefania Sarno, Maria Ruzzene, Anna Maria Brunati, Oriano Marin, Greg Vilk, Amanda Doherty-Kirby, Gilles Lajoie, David W Litchfield and 1 more

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

36 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
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  6. Review
  7. Article
  8. Article
  9. Insulin Receptor-Related Receptor Regulates the Rate of Early Development inInternational journal of molecular sciences · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Copper Modulates the Catalytic Activity of Protein Kinase CK2.Frontiers in molecular biosciences · 2022
    Article
  14. Review
  15. Article
  16. Targeting protein kinase CK2 in the treatment of cholangiocarcinoma.Exploration of targeted anti-tumor therapy · 2021
    Review
  17. Article
  18. Article
  19. Review
  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

11 authors at 2 institutions in 2 countries.

Arianna Donella-DeanaDipartimento di Chimica Biologica and CRIBI, Centro Nazionale delle Ricerche, Institute of Neuroscience, University of Padova, Viale G. Colombo 3, Italy.
Luca Cesaro
Stefania Sarno
Maria Ruzzene
Anna Maria Brunati
Oriano Marin
Greg Vilk
Amanda Doherty-Kirby
Gilles Lajoie
David W Litchfield
Lorenzo A Pinna
University of Padua · ITWestern University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Casein kinase-2 (CK2) is a pleiotropic and constitutively active serine/threonine protein kinase composed of two catalytic (alpha and/or alpha') and two regulatory beta-subunits, whose regulation is still not well understood. In the present study, we show that the catalytic subunits of human CK2, but not the regulatory beta-subunits, are readily phosphorylated by the Src family protein tyrosine kinases Lyn and c-Fgr to a stoichiometry approaching 2 mol phosphotyrosine/mol CK2alpha with a concomitant 3-fold increase in catalytic activity. We also show that endogenous CK2alpha becomes tyrosine-phosphorylated in pervanadate-treated Jurkat cells. Both tyrosine phosphorylation and stimulation of activity are suppressed by the specific Src inhibitor 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4- d ]pyrimidine. By comparison, mutations giving rise to inactive forms of CK2alpha do not abrogate and, in some cases, stimulate Lyn and c-Fgr-dependent tyrosine phosphorylation of CK2. Several radiolabelled phosphopeptides could be resolved by HPLC, following tryptic digestion of CK2alpha that had been phosphoradiolabelled by incubation with [(32)P]ATP and c-Fgr. The most prominent phosphopeptide co-migrates with a synthetic peptide encompassing the 248-268 sequence, phosphorylated previously by c-Fgr at Tyr(255) in vitro. The identification of Tyr(255) as a phosphorylated residue was also supported by MS sequencing of both the phosphorylated and non-phosphorylated 248-268 tryptic fragments from CK2alpha and by on-target phosphatase treatment. A CK2alpha mutant in which Tyr(255) was replaced by phenylalanine proved less susceptible to phosphorylation and refractory to stimulation by c-Fgr.

Indexed as

Amino Acid MotifsAnimalsCasein Kinase IICatalysisCatalytic DomainEnzyme InhibitorsHumansJurkat CellsMutationPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsPyrimidinesSequence Homology, Amino AcidAG 1879Casein Kinase IIEnzyme InhibitorsPhosphoproteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene Proteinsproto-oncogene proteins c-fgrPyrimidinessrc-Family KinasesTrypsinTyrosine

Identifiers

PMID12628006
PMCPMC1223437
OpenAlexW2020158668

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.