Isoform specific phosphorylation of p53 by protein kinase CK1

Venerando, Andrea; Marin, Oriano; Cozza, Giorgio; Bustos, Victor; Sarno, Stefania; Pinna, Lorenzo A.

doi:10.1007/s00018-009-0236-7

Cited by 34 publications

(28 citation statements)

References 63 publications

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“…This data agrees with the idea that some casein kinases participate in endoplasmic reticulum stress signaling via phosphorylation of different proteins which are important components of IRE-1 signaling [10,28,33]. We have found that the expression of different casein kinase-1 isoenzymes change in different ways in IRE-1α knockdown glioma cells and, it is quite possible, that this dysregulation is responsible for the suppression of proliferation of these cells [14], because different isoforms of casein kinase-1 (alpha, gamma-1, and delta) participate in the regulation of the Wnt and TGF-beta signaling cascades, in phosphorylation of TP53 [33,35,36]. Moreover, suppression of IRE-1α function in glioma cells also leads to a decrease of the catalytic subunit of casein kinase-2 (CSNK2A1) which has an important regulatory function in cell proliferation, cell differentiation, and in apoptosis via phosphorylation of a number of key intracellular signaling proteins implicated in tumorigenesis and tumor suppression [37].…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, CSNK1E is a crucial regulator of the Wnt signaling cascades, and breast cancer-specific mutations in this gene inhibit Wnt/beta-catenin and activate the Wnt/ Rac1/JNK and NFAT pathways to decrease cell adhesion and promote cell migration, thus contributing to breast cancer development via effects on cell adhesion and migration [33,34]. It was also shown that three isoforms of casein kinase-1 (alpha, gamma-1 and delta) participate in phosphorylation of the N-terminal region of TP53 [35]. There is data that casein kinase-1 gamma 2, an inhibitor of TGF-beta signaling, regulates ligand-dependent ubiquitynation of Smad3 [36].…”

Section: Introductionmentioning

confidence: 99%

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Expression of casein kinase genes in glioma cell line U87: Effect of hypoxia and glucose or glutamine deprivation

Minchenko¹,

Karbovskyi²,

Danilovskyi³

et al. 2012

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The endoplasmic reticulum-nuclei-1 (ERN1) sensing and signaling enzyme mediates a set of complex intracellular signaling events known as the unfolded protein response. We have studied the effect of hypoxia and ischemic conditions (glucose or glutamine deprivation) on the expression of several casein kinase-1 and -2 genes in glioma U87 cells and its subline with suppressed function of ERN1. It was shown that blockade of ERN1, the key endoplasmic reticulum stress sensor, leads to an increase in the expression levels of casein kinase-1G2, -1E, -2B and NUCKS1 mRNA, but suppresses casein kinase-1A1, -1D and -2A1. Moreover, the expression levels of casein kinase-1A1, -1D and 1G3 as well as casein kinase-2A1 and -2A2 mRNAs are significantly increased under glutamine deprivation conditions both in control and ERN1-deficient glioma cells. At the same time, casein kinase-1E, -2B and NUCKS1 mRNA expression levels are also increased under this condition, but only in cells with suppressed function of ERN1. The expression level of NUCKS1 mRNA, however, is decreased both in control glioma cells and in genetically modified cells, but casein kinase-1G2-only in control U87 cells. Cell exposure to glucose deprivation conditions enhances the expression levels of casein kinase-1D, 1G3, -1E and -2A1 in both types of glioma cells used, but casein kinase-2B expression levels increase only in cells with suppressed function of ERN1. Hypoxia induces or suppresses the expression of most of the studied genes mainly in ERN1-knockdown cells only. Results of this study show that hypoxia as well as glutamine and glucose deprivation conditions change the expression level most of casein kinase genes and that these effects are dependent on ERN1 signaling enzyme function.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Expression of casein kinase genes in glioma cell line U87: Effect of hypoxia and glucose or glutamine deprivation

Minchenko¹,

Karbovskyi²,

Danilovskyi³

et al. 2012

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“…CK1α, δ, and ε are able to phosphorylate certain N-terminal target sites of p53 (Ser-6, Ser-9, Ser-15, Thr-18, and Ser-20) (187, 234–237). By phosphorylation of p53 (mostly at Ser-15 and Thr-18) CK1δ and ε decrease p53 binding affinity to its cellular counterpart Mouse double-minute 2 homolog (MDM2) resulting in increased levels of MDM2-released, active p53 (234, 238, 239).…”

Section: Ck1 In Stress-related Cellular Functionsmentioning

confidence: 99%

“…The activation of Chk1 is supported by claspin whereas Chk1/claspin-binding is promoted by CK1γ1-mediated phosphorylation of claspin (162). The CK1 isoforms α, δ, and ε are able to activate p53 by site-specific phosphorylation (187, 234, 235, 237). Activated p53 in turn induces the expression of target genes like Bax (leading to apoptosis), p21 (leading to cell cycle arrest), and also CK1δ (autoregulatory feedback loop) (187).…”

Section: Ck1 In Stress-related Cellular Functionsmentioning

confidence: 99%

The CK1 Family: Contribution to Cellular Stress Response and Its Role in Carcinogenesis

et al. 2014

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Members of the highly conserved and ubiquitously expressed pleiotropic CK1 family play major regulatory roles in many cellular processes including DNA-processing and repair, proliferation, cytoskeleton dynamics, vesicular trafficking, apoptosis, and cell differentiation. As a consequence of cellular stress conditions, interaction of CK1 with the mitotic spindle is manifold increased pointing to regulatory functions at the mitotic checkpoint. Furthermore, CK1 is able to alter the activity of key proteins in signal transduction and signal integration molecules. In line with this notion, CK1 is tightly connected to the regulation and degradation of β-catenin, p53, and MDM2. Considering the importance of CK1 for accurate cell division and regulation of tumor suppressor functions, it is not surprising that mutations and alterations in the expression and/or activity of CK1 isoforms are often detected in various tumor entities including cancer of the kidney, choriocarcinomas, breast carcinomas, oral cancer, adenocarcinomas of the pancreas, and ovarian cancer. Therefore, scientific effort has enormously increased (i) to understand the regulation of CK1 and its involvement in tumorigenesis- and tumor progression-related signal transduction pathways and (ii) to develop CK1-specific inhibitors for the use in personalized therapy concepts. In this review, we summarize the current knowledge regarding CK1 regulation, function, and interaction with cellular proteins playing central roles in cellular stress-responses and carcinogenesis.

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“…The kinase is composed of a tetramer of α, α’, and two β subunits [47, 48]. The PrimePCR assays showed that casein kinase 2 α1 (CSNK2A1) was significantly upregulated in T 3 -treated differentiated LNCaP cells (Fig.…”

Section: Introductionmentioning

confidence: 99%

New insights on thyroid hormone mediated regulation of herpesvirus infections

Figliozzi

Chen

2017

Cell Biosci

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Thyroid hormone (T3) has been suggested to participate in the regulation of herpesvirus replication during reactivation. Clinical observations and in vivo experiments suggest that T3 are involved in the suppression of herpes virus replication. In vitro, differentiated LNCaP cells, a human neuron-like cells, further resisted HSV-1 replication upon addition of T3. Previous studies indicate that T3 controlled the expression of several key viral genes via its nuclear receptors in differentiated LNCaP cells. Additional observation showed that differentiated LNCaP cells have active PI3K signaling and inhibitor LY294002 can reverse T3-mediated repression of viral replication. Active PI3K signaling has been linked to HSV-1 latency in neurons. The hypothesis is that, in addition to repressing viral gene transcription at the nuclear level, T3 may influence PI3K signaling to control HSV-1 replication in human neuron-like cells. We review the genomic and non-genomic regulatory roles of T3 by examining the phosphoinositide 3-kinase (PI3K) pathway gene expression profile changes in differentiated LNCaP cells under the influence of hormone. The results indicated that 15 genes were down-regulated and 22 genes were up-regulated in T3-treated differentiated LNCaP cells in comparison to undifferentiated state. Of all these genes, casein kinase 2 (CK2), a key component to enhance PI3K signaling pathway, was significantly increased upon T3 treatment only while the cells were differentiated. Further studies revealed that CK2 inhibitors tetrabrominated cinnamic acid (TBCA) and 4, 5, 6, 7-tetrabromo-2H-benzotriazole (TBB) both reversed the T3-mediated repression of viral replication. Together these observations suggested a new approach to understanding the roles of T3 in the complicated regulation of HSV-1 replication during latency and reactivation.Electronic supplementary materialThe online version of this article (doi:10.1186/s13578-017-0140-z) contains supplementary material, which is available to authorized users.

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Isoform specific phosphorylation of p53 by protein kinase CK1

Cited by 34 publications

References 63 publications

Expression of casein kinase genes in glioma cell line U87: Effect of hypoxia and glucose or glutamine deprivation

Expression of casein kinase genes in glioma cell line U87: Effect of hypoxia and glucose or glutamine deprivation

The CK1 Family: Contribution to Cellular Stress Response and Its Role in Carcinogenesis

New insights on thyroid hormone mediated regulation of herpesvirus infections

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