ArticleThe Biochemical journal2006
The N-terminal domain of the human eIF2beta subunit and the CK2 phosphorylation sites are required for its function.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Premeiotic deletion of Eif2s2 causes oocyte arrest at the early diplotene stage and apoptosis in mice.Cell proliferation · 2024Article
- Casein kinase 2 phosphorylates and induces the SALL2 tumor suppressor degradation in colon cancer cells.Cell death & disease · 2024Article
- Inhibition of casein kinase 2 sensitizes mantle cell lymphoma to venetoclax through MCL-1 downregulation.Haematologica · 2023Article
- Phosphoproteomic Landscape of AML Cells Treated with the ATP-Competitive CK2 Inhibitor CX-4945.Cells · 2021Article
- Signaling Pathways Involved in the Regulation of mRNA Translation.Molecular and cellular biology · 2018Review
- 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
- Phosphoproteomics of colon cancer metastasis: comparative mass spectrometric analysis of the isogenic primary and metastatic cell lines SW480 and SW620.Analytical and bioanalytical chemistry · 2017Article
- Identification of Candidate Casein Kinase 2 Substrates in Mitosis by Quantitative Phosphoproteomics.Frontiers in cell and developmental biology · 2017Article
- mTORC1 and CK2 coordinate ternary and eIF4F complex assembly.Nature communications · 2016Article
- Identification of Plasmodium falciparum Translation Initiation eIF2β Subunit: Direct Interaction with Protein Phosphatase Type 1.Frontiers in microbiology · 2016Article
- Phosphorylation stoichiometries of human eukaryotic initiation factors.International journal of molecular sciences · 2014Article
- Cross-species proteomics reveals specific modulation of signaling in cancer and stromal cells by phosphoinositide 3-kinase (PI3K) inhibitors.Molecular & cellular proteomics : MCP · 2014Article
- Why is start codon selection so precise in eukaryotes?Translation (Austin, Tex.) · 2014Review
- Identification of the phosphorylated residues in TveIF5A by mass spectrometry.Genomics, proteomics & bioinformatics · 2013Article
- Article
- Phosphorylation of maize eukaryotic translation initiation factor 5A (eIF5A) by casein kinase 2: identification of phosphorylated residue and influence on intracellular localization of eIF5A.The Journal of biological chemistry · 2010Article
- Phosphorylation of plant translation initiation factors by CK2 enhances the in vitro interaction of multifactor complex components.The Journal of biological chemistry · 2009Article
- Differential phosphorylation of plant translation initiation factors by Arabidopsis thaliana CK2 holoenzymes.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CK2 (protein kinase CK2) is known to phosphorylate eIF2 (eukaryotic translation initiation factor 2) in vitro; however, its implication in this process in living cells has remained to be confirmed. The combined use of chemical inhibitors (emodin and apigenin) of CK2 together with transfection experiments with the wild-type of the K68A kinase-dead mutant form of CK2alpha evidenced the direct involvement of this protein kinase in eIF2beta phosphorylation in cultured HeLa cells. Transfection of HeLa cells with human wild-type eIF2beta or its phosphorylation site mutants showed Ser2 as the main site for constitutive eIF2beta phosphorylation, whereas phosphorylation at Ser67 seems more restricted. In vitro phosphorylation of eIF2beta also pointed to Ser2 as a preferred site for CK2 phosphorylation. Overexpression of the eIF2beta S2/67A mutant slowed down the rate of protein synthesis stimulated by serum, although less markedly than the overexpression of the Delta2-138 N-terminal-truncated form of eIF2beta (eIF2beta-CT). Mutation at Ser2 and Ser67 did not affect eIF2beta integrating into the eIF2 trimer or being able to complex with eIF5 and CK2alpha. The eIF2beta-CT form was also incorporated into the eIF2 trimer but did not bind to eIF5. Overexpression of eIF2beta slightly decreased HeLa cell viability, an effect that was more evident when overexpressing the eIF2beta S2/67A mutant. Cell death was particularly marked when overexpressing the eIF2beta-CT form, being detectable at doses where eIF2beta and eIF2beta S2/67A were ineffective. These results suggest that Ser2 and Ser67 contribute to the important role of the N-terminal region of eIF2beta for its function in mammals.
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