ArticleMolecular and cellular biochemistry2008
Cell cycle and activation of CK2.
Article in Molecular and cellular biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 45 citations in OpenAlex.
- Circadian Control of Protein Synthesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Hyperphosphorylation of hepatic proteome characterizes nonalcoholic fatty liver disease in S-adenosylmethionine deficiency.iScience · 2023Article
- Yeast Protein Asf1 Possesses Modulating Activity towards Protein Kinase CK2.International journal of molecular sciences · 2022Article
- Inhibition of Protein Kinase CK2 Affects Thymidylate Synthesis Cycle Enzyme Level and Distribution in Human Cancer Cells.Frontiers in molecular biosciences · 2022Article
- CK2 Regulation: Perspectives in 2021.Biomedicines · 2021Review
- CK2-mediated phosphorylation of Che-1/AATF is required for its pro-proliferative activity.Journal of experimental & clinical cancer research : CR · 2021Article
- Synthesis of Novel Acyl Derivatives of 3-(4,5,6,7-Tetrabromo-1International journal of molecular sciences · 2021Article
- The Keap1-Nrf2 System: A Mediator between Oxidative Stress and Aging.Oxidative medicine and cellular longevity · 2021Review
- Potential role of PIN1 genotypes in predicting benefit from oxaliplatin-based and irinotecan-based treatment in patients with metastatic colorectal cancer.The pharmacogenomics journal · 2018Article
- Protein Kinase CK2: Intricate Relationships within Regulatory Cellular Networks.Pharmaceuticals (Basel, Switzerland) · 2017Review
- A Herpesviral induction of RAE-1 NKG2D ligand expression occurs through release of HDAC mediated repression.eLife · 2016Article
- Role of Eukaryotic Initiation Factors during Cellular Stress and Cancer Progression.Journal of nucleic acids · 2016Review
- Regulation of ceramide synthase by casein kinase 2-dependent phosphorylation in Saccharomyces cerevisiae.The Journal of biological chemistry · 2015Article
- MEK inhibitor PD-0325901 overcomes resistance to CK2 inhibitor CX-4945 and exhibits anti-tumor activity in head and neck cancer.International journal of biological sciences · 2015Article
- Article
- Regulation of CK2 by phosphorylation and O-GlcNAcylation revealed by semisynthesis.Nature chemical biology · 2012Article
- Threonine 393 of beta-catenin regulates interaction with Axin.Journal of cellular biochemistry · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Casein kinase 2 (CK2) is a highly conserved and ubiquitous eukaryotic Ser/Thr protein kinase. Genetic, biochemical, and cell biological studies have indicated the involvement of this enzyme in the control of cell proliferation and in signal transduction. The regulation of CK2 is not well defined, and it has been considered a constitutively non-regulated protein kinase. However, we show that CK2 activation occurred during the progression of cell cycle in response to FBS stimuli of G0 arrested cells. Importantly, we show that as the downstream target for CK2, the phosphorylation of eukaryotic translation-initiation factor eIF5 by CK2 may play a critical role in cell cycle progression. We find that eIF5 is associated with CK2 when the kinase activity is at the highest level in vivo, and is phosphorylated at Ser389 and Ser390 by CK2. Expression of eIF5 mutants that lack those phosphorylation sites reveals that these mutants have a dominant-negative effect on phosphorylation of endogenous eIF5, as well as a significant reduction in the formation of the mature complex, in the growth rate, and the expression of cell cycle-regulated proteins. Also, a pool of CK2 translocates into the nuclear fraction following its activation during the progression of the cell cycle. Consistent with these findings, we report that CK2 may be involved in the regulation of cell cycle progression through the phosphorylation of a key molecule for translation initiation and of nuclear substrates upon activation of CK2 by itself.
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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.