ArticleThe Biochemical journal2003
Eukaryotic translation-initiation factor eIF2beta binds to protein kinase CK2: effects on CK2alpha activity.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- Placental Mammals Acquired Functional Sequences in NRK for Regulating the CK2-PTEN-AKT Pathway and Placental Cell Proliferation.Molecular biology and evolution · 2022Article
- Chemical Genetic Validation of CSNK2 Substrates Using an Inhibitor-Resistant Mutant in Combination with Triple SILAC Quantitative Phosphoproteomics.Frontiers in molecular biosciences · 2022Article
- Development of a potent and selective chemical probe for the pleiotropic kinase CK2.Cell chemical biology · 2021Article
- Synthesis and SAR of Tetracyclic Inhibitors of Protein Kinase CK2 Derived from Furocarbazole W16.ChemMedChem · 2020Article
- Article
- Ecto-protein kinase CK2, the neglected form of CK2.Biomedical reports · 2018Review
- Under-expression of CK2β subunit in ccRCC represents a complementary biomarker of p-STAT3 Ser727 that correlates with patient survival.Oncotarget · 2018Article
- Deletion of eIF2β lysine stretches creates a dominant negative that affects the translation and proliferation in human cell line: A tool for arresting the cell growth.Cancer biology & therapy · 2017Article
- Dissecting the roles of tyrosines 490 and 785 of TrkA protein in the induction of downstream protein phosphorylation using chimeric receptors.The Journal of biological chemistry · 2013Article
- Interactions between subunits of protein kinase CK2 and their protein substrates influences its sensitivity to specific inhibitors.Molecular and cellular biochemistry · 2011Article
- Article
- Ability of CK2beta to selectively regulate cellular protein kinases.Molecular and cellular biochemistry · 2008Article
- The translation initiation factor eIF2beta is an interactor of protein phosphatase-1.The Biochemical journal · 2006Article
- The N-terminal domain of the human eIF2beta subunit and the CK2 phosphorylation sites are required for its function.The Biochemical journal · 2006Article
- Cross talk between protein kinase CK2 and eukaryotic translation initiation factor eIF2beta subunit.Molecular and cellular biochemistry · 2005Article
- Protein kinase CK2 phosphorylation regulates the interaction of Kaposi's sarcoma-associated herpesvirus regulatory protein ORF57 with its multifunctional partner hnRNP K.Nucleic acids research · 2004Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
eIF2 (eukaryotic translation-initiation factor 2) is a substrate and an interacting partner for CK2 (protein kinase CK2). Co-immuno-precipitation of CK2 with eIF2beta has now been observed in HeLa cells, overexpressing haemagglutinin-tagged human recombinant eIF2beta. A direct association between His6-tagged human recombinant forms of eIF2beta subunit and both the catalytic (CK2alpha) and the regulatory (CK2beta) subunits of CK2 has also been shown by using different techniques. Surface plasmon resonance analysis indicated a high affinity in the interaction between eIF2beta and CK2alpha, whereas the affinity for the association with CK2beta is much lower. Free CK2alpha is unable to phosphorylate eIF2beta, whereas up to 1.2 mol of phosphate/mol of eIF2beta was incorporated by the reconstituted CK2 holoenzyme. The N-terminal third part of eIF2beta is dispensable for binding to either CK2alpha or CK2beta, although it contains the phosphorylation sites for CK2. The remaining central/C-terminal part of eIF2beta is not phosphorylated by CK2, but is sufficient for binding to both CK2 subunits. The presence of eIF2beta inhibited CK2alpha activity on calmodulin and beta-casein, but it had a minor effect on that of the reconstituted CK2 holoenzyme. The truncated forms corresponding to the N-terminal or central/C-terminal regions of eIF2beta were much less inhibitory than the intact subunit. The results demonstrate that the ability to associate with CK2 subunits and to serve as a CK2 substrate are confined to different regions in eIF2beta and that it may act as an inhibitor on CK2alpha.
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