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Analysis of gene expression changes in fetal erythroid cells obtained from mice with Csnk2b gene conditional deletion in the hematopoietic system.

ABSTRACT: Protein Kinase CK2 is a pleiotropic and constitutively expressed enzyme (phosphotransferase) usually present as a tetrameric complex of two catalytic alpha and two regulatory beta subunits. Alpha and beta proteins can also work independently from the holoenzyme exerting different functions on other protein targets. It is well known the CK2 role in promoting cell survival and proliferation and in sustaining the growth of many hematological malignances. However, its physiological role in hematopoiesis, in particular in erythropoiesis is still unknown. Our analysis was focused on the hematopoietic functions of the beta subunit through the generation of conditional KO mice for Csnk2b gene in the hematopoietic system. Our purpose was to asses if CK2b plays a role in the development of erythroid cells. To this aim, we performed a mRNA sequencing analysis of erythroid TER119+ cells purified from control (Csnk2b+/+) and KO (Csnk2b-/-) embryos and here we report a complete list of the genes resulted to be differentially expressed.

ORGANISM(S): Mus musculus

PROVIDER: GSE158665 | GEO | 2022/09/30

REPOSITORIES: GEO

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Analysis of gene expression changes in B cells upon Csnk2b conditional deletion

Project description:Protein kinase CK2, a tetrameric enzyme composed by 2 catalitic alpha and 2 regulatory beta subunits, supports malignant B cell lymphocyte growth, however, its physiological role in B lymphopoiesis is still unknown. With this analysis we intended to assess if CK2 plays a role in peripheral B cell development and to do this we compared the mRNA from Csnk2b+/+ (WT) and Csnk2b-/- (KO) purified splenic B cells. Here we report a list of all genes identified as differentially expressed between WT and KO B cells.

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CK2β is a gatekeeper of focal adhesions regulating cell spreading

Project description:CK2 is an hetero-tetrameric protein made of two CK2α catalytic subunits and two regulatory CK2β subunits. The free CK2α subunit and the tetrameric holoenzyme have distinct substrate specificity profiles suggesting that the spatiotemporal organization of the individual CK2 subunits observed in living cells is crucial in the control of the many cellular processes that are governed by this pleiotropic kinase. Indeed, sub-stoichiometric expression of CK2β compared to CK2α in a subset of breast cancer tumors was correlated with the induction of EMT markers and increased epithelial cell plasticity in breast carcinoma progression. Using phosphotyrosine profiling with affinity capture and LC/MS-MS, we show that decreased expression of CK2β in MCF10A mammary epithelial cells triggers the phosphorylation of a number of tyrosine phosphorylated proteins and promotes the striking activation of the FAK1-Src-PAX1 signaling pathway. Moreover, morphometric analyses also revealed that CK2β loss increases the number and the spatial distribution of focal adhesion signaling complexes. Together, our finding allows positioning CK2β as a gatekeeper for cell spreading by restraining the focal adhesion maturation and invasion of mammary epithelial cells.

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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.

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Stem cell-like properties of CK2β-downregulated mammary cells [mRNA]

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Substrate selectivity for semisynthetic CK2 proteins with various posttranslational modifications

2011-10-25 | GSE33149 | GEO

Liquid chromatography-mass spectrometry analysis of an in vitro phosphorylation assay

Project description:Liquid chromatography (LC)-mass spectrometry analysis of an in vitro phosphorylation assay with the recombinant CK2 holoenzyme and ECT peptide in the absence or presence of CX-4945 (10 µM, 4 hr)

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KLF1/EKLF regulatory networks in primary erythroid cells

Project description:KLF1 (EKLF) regulates a diverse suite of genes to direct erythroid cell differentiation from bi-potent progenitors. To determine the local cis-regulatory contexts and transcription factor networks in which KLF1 operates, we performed KLF1 ChIP-seq in the mouse. We found at least 945 sites in the genome of E14.5 fetal liver erythroid cells which are occupied by endogenous KLF1. Many of these recovered sites reside in erythroid gene promoters such as β-globin, but the majority are distant to any known gene. Our data suggests KLF1 directly regulates most aspects of terminal erythroid differentiation including production of α and β-globin protein chains, heme biosynthesis, co-ordination of proliferation and anti-apoptotic pathways, and construction of the red cell membrane and cytoskeleton by functioning primarily as a transcriptional activator. Additionally, we suggest new mechanisms for KLF1 co-operation with other transcription factors, in particular the erythroid transcription factor GATA1, to maintain homeostasis in the erythroid compartment. Examination of KLF1 occupancy in primary erythroid cells. KLF1-ChIP and input samples were run on AB SOLiD Systems 2.0 and 3.0. The genomic alignment files (*sorted.txt) and peak file (*bed) contain the combined System 2.0 and 3.0 data.

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