ArticleOncogene2003
Protein kinase CK2 regulates CDC25B phosphatase activity.
Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 73 citations in OpenAlex.
- CK2 activity is crucial for proper glucagon expression.Diabetologia · 2024Article
- CK2β Regulates Hematopoietic Stem Cell Biology and Erythropoiesis.HemaSphere · 2023Article
- Review
- Comparing Two Neurodevelopmental Disorders Linked to CK2: Okur-Chung Neurodevelopmental Syndrome and Poirier-Bienvenu Neurodevelopmental Syndrome-Two Sides of the Same Coin?Frontiers in molecular biosciences · 2022Review
- Oxidative stress induces Ser 2 dephosphorylation of the RNA polymerase II CTD and premature transcription termination.Transcription · 2021Article
- Identification of Candidate Casein Kinase 2 Substrates in Mitosis by Quantitative Phosphoproteomics.Frontiers in cell and developmental biology · 2017Article
- Quantitative phosphoproteomics reveals new roles for the protein phosphatase PP6 in mitotic cells.Science signaling · 2015Article
- Unconventional Functions of Mitotic Kinases in Kidney Tumorigenesis.Frontiers in oncology · 2015Review
- Kizuna is a novel mitotic substrate for CDC25B phosphatase.Cell cycle (Georgetown, Tex.) · 2014Article
- CDC25B overexpression stabilises centrin 2 and promotes the formation of excess centriolar foci.PloS one · 2013Article
- Down-regulation of CK2 activity results in a decrease in the level of cdc25C phosphatase in different prostate cancer cell lines.Molecular and cellular biochemistry · 2011Article
- A specific inhibitor of protein kinase CK2 delays gamma-H2Ax foci removal and reduces clonogenic survival of irradiated mammalian cells.Radiation oncology (London, England) · 2011Article
- Human Cdc14A phosphatase modulates the G2/M transition through Cdc25A and Cdc25B.The Journal of biological chemistry · 2010Article
- Mitotic phosphorylation of Cdc25B Ser321 disrupts 14-3-3 binding to the high affinity Ser323 site.The Journal of biological chemistry · 2010Article
- MAPK pathway activation delays G2/M progression by destabilizing Cdc25B.The Journal of biological chemistry · 2009Article
- An integrated comparative phosphoproteomic and bioinformatic approach reveals a novel class of MPM-2 motifs upregulated in EGFRvIII-expressing glioblastoma cells.Molecular bioSystems · 2009Article
- Ability of CK2beta to selectively regulate cellular protein kinases.Molecular and cellular biochemistry · 2008Article
- A novel role for PA28gamma-proteasome in nuclear speckle organization and SR protein trafficking.Molecular biology of the cell · 2008Article
- Small interfering RNA targeting CDC25B inhibits liver tumor growth in vitro and in vivo.Molecular cancer · 2008Article
- Structure-based design of small peptide inhibitors of protein kinase CK2 subunit interaction.The Biochemical journal · 2007Article
Corrections and comments
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Authors and funding
8 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human dual-specificity phosphatases CDC25 (A, B and C) play an important role in the control of cell cycle progression by activating the cyclin-dependent kinases (CDKs). Regulation of these phosphatases during the cell cycle involves post-translational modifications such as phosphorylation and protein-protein interactions. Given the suspected involvement of the protein kinase CK2 at the G2/M transition, we have investigated its effects on the CDC25B phosphatase. We show that in vitro CK2 phosphorylates CDC25B, but not CDC25C. Mass spectrometry analysis demonstrates that at least two serine residues, Ser-186 and Ser-187, are phosphorylated in vivo. We also report that CDC25B interacts with CK2, and this interaction, mediated by the CK2beta regulatory subunit, involves domains that are located within the first 55 amino acids of CK2beta and between amino acids 122 and 200 on CDC25B. This association was confirmed in vivo, in Sf9 insect cells and in U(2)OS human cells expressing an HA epitope-tagged CDC25B. Finally, we demonstrate that phosphorylation of CDC25B by protein kinase CK2 increases the catalytic activity of the phosphatase in vitro as well as in vivo. We discuss the possibility that CDC25B phosphorylation by CK2 could play a role in the regulation of the activity of CDC25B as a starter of mitosis.
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Registered trials
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.