Cell cycle-dependent gene networks for cell proliferation activated by nuclear CK2 complexes [array]
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA946735 | ENA |
REPOSITORIES: ENA
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 CK2α to the active gene locus, more abundantly in late G1 phase than in early G1. We analyzed the transcriptome of RPE wt and CK2α-ko cells, both arrested in early and late G1 during progression of the cell cycle. This study suggests that nuclear CK2α complexes, uniquely constituted during cell cycle progression, are essential for cell proliferation, by activating genes and synthesizing components necessary for cell division, specified in the nucleus and nucleolus.
2023-10-19 | GSE227739 | GEO
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:Cell cycle-dependent gene networks for cell proliferation activated by nuclear CK2 complexes
| PRJNA941788 | ENA
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:Maf-family basic motif leucine zipper protein NRL specifies rod photoreceptor cell fate during retinal development and, in concert with homeodomain protein CRX and other regulatory factors, controls the expression of most rod-expressed genes including the visual pigment gene RHO (rhodopsin). Transcriptional regulatory activity of NRL is modulated by post-translational modifications (PTMs), specially phosphorylation, and mutations in phosphosites can lead to retinal degeneration. During our studies to elucidate NRL-mediated transcriptional regulation, we identified Protein Kinase CK2 in NRL-enriched complexes bound to RHO promoter-enhancer regions and in NRL-enriched high molecular mass fractions from the bovine retina. The presence of CK2 in NRL complexes was confirmed by co-immunoprecipitation from developing and adult mouse retinal extracts. Bioinformatic and mass spectrometry analysis indicated potential phosphorylation of NRL at Ser117 residue by CK2. Co-transfection of Csnk2a1 cDNA encoding CK2 with NRL and CRX reduced the bovine Rho promoter-driven luciferase expression in HEK293 cells, and mutagenesis of NRL-Ser117 residue to Ala restored the reporter gene expression. In concordance, overexpression of CK2 in the mouse retina in vivo by electroporation resulted in reduction of Rho promoter-driven DsRed reporter gene expression. RNA-seq analysis of CK2-electroporated retina revealed altered expression of many transcriptional targets of NRL. Thus, our studies demonstrate an important role of CK2 in context-dependent fine-tuning of NRL function, consequently modulating the expression of rod photoreceptor genes.
2024-04-06 | GSE171665 | 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
Project description: Not available
| S-EPMC10618106 | biostudies-literature
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:This SuperSeries is composed of the following subset Series: GSE33149: Substrate selectivity for semisynthetic CK2 proteins with various posttranslational modifications GSE33150: Substrate selectivity for semisynthetic CK2 proteins with Pin1 Refer to individual Series
2011-10-24 | E-GEOD-33151 | biostudies-arrayexpress