Cell cycle-dependent gene networks for cell proliferation activated by nuclear CK2 complexes [array]
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ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE227739 | GEO | 2023/10/19
REPOSITORIES: GEO
Similar Datasets
Project description:Protein kinase CK2 is a conserved serine/threonine kinase that participates in various cellular processes. Chromatin immunoprecipitation-sequencing profiling demonstrated recruitment of CK2alpha to the active gene locus, more abundantly in late G1 phase than in early G1. Notably, we confirmed the presence of CK2alpha at transcriptional start sites of core histone genes, growth stimulus-associated genes, and ribosomal RNAs. This study suggests that nuclear CK2alpha complexes, uniquely constituted during cell cycle progression, are essential for cell proliferation, by activating histone genes, triggering ribosome biogenesis, and synthesizing components necessary for cell division, specified in the nucleus and nucleolus.
2023-10-19 | GSE226778 | GEO
Project description:Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is phosphorylated at Thr344 and phosphorylation on the C-terminal tail of CK2α is required for interaction with Pin1 protein. The substrate selectivity for protein kinase CK2α was examined by performing kinase assays on protein microarrays spotted with 17,000 human proteins. Semisynthetic CK2α proteins were prepared to contain an unmodified C-terminal tail or phospho-Thr (pThr) at T344. These semisynthetic proteins were used to determine if the phosphorylation-dependent interaction of CK2α with Pin1 can modulate the substrate selectivity for CK2. The different semisynthetic CK2α proteins (unmodified and pThr344) were tested alone and in the presence of the recombinant Pin1 protein. Pin1 has been shown to interaction with CK2α only when CK2α is phoshorylated on its C-terminal site (including Thr344). In the study presented here, kinase assays were performed using two different semisynthetic CK2α proteins: unmodified C-terminal tail and phospho-Thr (pThr) at 344. The semisynthetic proteins were each tested alone and in the presence of the recombinant Pin1 protein. There were four different kinase conditions and each condition was performed in duplicate.
2011-10-24 | E-GEOD-33150 | biostudies-arrayexpress
Project description:Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is phosphorylated at Thr344 and phosphorylation on the C-terminal tail of CK2α is required for interaction with Pin1 protein. The substrate selectivity for protein kinase CK2α was examined by performing kinase assays on protein microarrays spotted with 17,000 human proteins. Semisynthetic CK2α proteins were prepared to contain an unmodified C-terminal tail or phospho-Thr (pThr) at T344. These semisynthetic proteins were used to determine if the phosphorylation-dependent interaction of CK2α with Pin1 can modulate the substrate selectivity for CK2. The different semisynthetic CK2α proteins (unmodified and pThr344) were tested alone and in the presence of the recombinant Pin1 protein. Pin1 has been shown to interaction with CK2α only when CK2α is phoshorylated on its C-terminal site (including Thr344).
2011-10-25 | GSE33150 | GEO
Project description:Protein kinase CK2 is a conserved serine/threonine kinase that participates in various cellular processes. Elevated nuclear expression of CK2α has been observed in human carcinomas, but mechanisms for its variable localization in cells are poorly understood. This study demonstrates a functional connection between nuclear CK2 and gene expression in relation to cell proliferation. Growth stimulation of quiescent human fibroblasts identified a pool of CK2 highly phosphorylated at serine 7 of the α subunit that translocated into the nucleus. This phosphorylation appeared essential for its nuclear localization and catalytic activity. Protein signatures associated with nuclear CK2 complexes revealed enrichment of transcription factors and chromatin remodelers that seemed unique during progression through G1 phase of the cell cycle. Chromatin immunoprecipitation-sequencing profiling demonstrated recruitment of CK2α to the active gene locus, more abundantly in late G1 phase than in early G1. Notably, we confirmed the presence of CK2α at transcriptional start sites of core histone genes, growth stimulus-associated genes, and ribosomal RNAs. This study suggests that nuclear CK2α complexes, uniquely constituted during cell cycle progression, are essential for cell proliferation, by activating histone genes, triggering ribosome biogenesis, and then synthesize the components necessary for cell division, specified in the nucleus and also in the nucleolus.
2023-10-22 | PXD040882 | JPOST Repository
Project description:Protein kinase CK2 is a conserved serine/threonine kinase that participates in various cellular processes. Elevated nuclear expression of CK2α has been observed in human carcinomas, but mechanisms for its variable localization in cells are poorly understood. This study demonstrates a functional connection between nuclear CK2 and gene expression in relation to cell proliferation. Growth stimulation of quiescent human fibroblasts identified a pool of CK2 highly phosphorylated at serine 7 of the α subunit that translocated into the nucleus. This phosphorylation appeared essential for its nuclear localization and catalytic activity. Protein signatures associated with nuclear CK2 complexes revealed enrichment of transcription factors and chromatin remodelers that seemed unique during progression through G1 phase of the cell cycle. Chromatin immunoprecipitation-sequencing profiling demonstrated recruitment of CK2α to the active gene locus, more abundantly in late G1 phase than in early G1. Notably, we confirmed the presence of CK2α at transcriptional start sites of core histone genes, growth stimulus-associated genes, and ribosomal RNAs. This study suggests that nuclear CK2α complexes, uniquely constituted during cell cycle progression, are essential for cell proliferation, by activating histone genes, triggering ribosome biogenesis, and then synthesize the components necessary for cell division, specified in the nucleus and also in the nucleolus.
2024-10-22 | PXD046282 | JPOST Repository
Project description:Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is modified by O-GlcNAc on Ser347 proximal to a Cdk1 phosphorylation site at Thr344 on the same protein. The substrate selectivity for protein kinase CK2 was examined by performing kinase assays on protein microarrays spotted with 17,000 human proteins. Semisynthetic CK2α proteins were prepared to contain an unmodified C-terminal tail, S-GlcNAc-Serine at S347, or Pfa (non-hyrdolyzeable phosphomimic) at T344. These semisynthetic proteins were used to determine if the posttranslational modifications on CK2 alpha modulate the substrate selectivity for this pleiotropic kinase. The different semisynthetic CK2α proteins were tested alone and in the presence of the regulatory subunit CK2β since it is known that the CK2α subunit is active both in its isolated state and in the heterotetrameric state formed in the presence of the regulatory beta subunit. The CK2β subunit has been shown to modulate CK2 activity with some substrates and not others. In the study presented here, kinase assays were performed using three different semisynthetic CK2 alpha proteins: unmodified C-terminal tail; S-GlcNAc-Ser at 347; and Pfa (phosphomimic) at 344. The semisynthetic proteins were each tested alone and in the presence of the regualatory CK2 beta subunit. There were six different kinase conditions and each condition was performed in duplicate and one no kinase control was performed to eliminate autophorylated proteins.
2011-10-24 | E-GEOD-33149 | biostudies-arrayexpress
Project description:Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is modified by O-GlcNAc on Ser347 proximal to a Cdk1 phosphorylation site at Thr344 on the same protein. The substrate selectivity for protein kinase CK2 was examined by performing kinase assays on protein microarrays spotted with 17,000 human proteins. Semisynthetic CK2α proteins were prepared to contain an unmodified C-terminal tail, S-GlcNAc-Serine at S347, or Pfa (non-hyrdolyzeable phosphomimic) at T344. These semisynthetic proteins were used to determine if the posttranslational modifications on CK2 alpha modulate the substrate selectivity for this pleiotropic kinase. The different semisynthetic CK2α proteins were tested alone and in the presence of the regulatory subunit CK2β since it is known that the CK2α subunit is active both in its isolated state and in the heterotetrameric state formed in the presence of the regulatory beta subunit. The CK2β subunit has been shown to modulate CK2 activity with some substrates and not others.
2011-10-25 | GSE33149 | GEO
Project description:Protein kinase 2 (CK2) is a serine/threonine kinase composed of two catalytic subunits (CK2α and/or CK2α') and two regulatory subunits (CK2β). CK2 has been shown to promote cancer progression by regulating the NF-κB, PI3K/AKT/mTOR, JAK/STAT and HIF-1α pathways, and also plays a critical role for immune cell development and function. However, the potential involvement of CK2 in CD8+ T-cell function has not explored. Here, we demonstrate that CK2 protein levels and kinase activity are enhanced upon CD8+ T-cell activation. CK2α deficiency results in impaired CD8+ T-cell activation and proliferation upon TCR stimulation. Furthermore, CK2α is involved in CD8+ T-cell metabolic reprogramming during activation through regulating the AKT/mTOR signaling pathway. Lastly, using a Listeria monocytogenes infection model, we demonstrate that CK2α is required for CD8+ T-cell expansion, maintenance and effector function in both primary and memory immune responses. Taken together, our study implicates CK2 as an important regulator of CD8+ T-cell activation and differentiation both in vitro and in vivo.
2022-06-21 | GSE175941 | GEO
Project description:Preadipocytes initiate differentiation into adipocytes through a cascade of events. Mitotic clonal expansion, as one of the earliest event, is essential for adipogenesis. However, the underlying mechanisms that regulate mitotic clonal expansion remain elusive. SIRT6 is a member of the evolutionarily conserved sirtuin family of NAD+ dependent protein deacetylases and plays roles in genomic stability, aging, glucose metabolism and inflammatory response. Here, we show that SIRT6 deficiency in preadipocytes blocked their adipogenesis. Analysis of gene expression during adipogenesis reveals that KIF5C, which belongs to kinesin family, is negatively regulated by SIRT6. Furthermore, we show that KIF5C is a negative factor for adipogenesis through interacting with CK2α’, a catalytic subunit of CK2. This interaction blocks CK2α’ nuclear translocation and CK2 kinase activity, and inhibits mitotic clonal expansion during adipogenesis. Thus, SIRT6 acts as an important factor of adipogenesis through inhibiting KIF5C expression and enhancing CK2 kinase activity.
2018-01-16 | GSE94058 | GEO
Project description:CK2 binds to actively transcribed regions in the genome and regulates transcriptional elongation. Identification of genome-wide binding sites of CK2?, and examination of the effect of Pol II binding upon CK2 inhibition in LNCaP cells
2014-09-30 | E-GEOD-58607 | biostudies-arrayexpress