Protein kinase CK2 (“casein kinase-2”) and its implication in cell division and proliferation

Pinna, Lorenzo A.; Meggio, Flavio

doi:10.1007/978-1-4615-5371-7_7

Cited by 317 publications

(289 citation statements)

References 190 publications

(168 reference statements)

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“…Inhibition of phosphorylation, for example in the presence of DRB, would allow hydroxylation and inhibit HIF-1 activity. Two-hybrid screening in yeast has shown that CK2b has several binding partners, among them the collagen a-prolyl-4 hydroxylase, 58,59 but the mechanisms of their interaction as well as the functional consequence of the interaction are currently poorly understood, as is the question of whether CK2 would also interact with the HIF prolyl hydroxylase. The use of antibodies that could recognize the hydroxylated N803 would be helpful to confirm this hypothesis.…”

Section: Discussionmentioning

confidence: 99%

Role for casein kinase 2 in the regulation of HIF‐1 activity

Mottet

Ruys

Demazy

et al. 2005

Intl Journal of Cancer

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Hypoxia-inducible factor-1 (HIF-1) is a heterodimeric transcription factor that plays a major role in cellular adaptation to hypoxia. The mechanisms regulating HIF-1 activity occurs at multiple levels in vivo. The HIF-1a subunit is highly sensible to oxygen and is rapidly degraded by the proteasome 26S in normoxia. Activation in hypoxia occurs through a multistep process including inhibition of HIF-1a degradation, but also increase in the transactivation activity of HIF-1. Several data indicate that phosphorylation could play a role in this regulation. In this report, we investigated the role of casein kinase 2 (CK2), an ubiquitous serine/ threonine kinase, in the regulation of HIF-1 activity. Hypoxia was capable of increasing the expression of the b subunit of CK2, of inducing a relocalization of this subunit at the plasma membrane, of inducing nuclear translocation of the a subunit and of increasing CK2 activity. Three inhibitors of this kinase, DRB (5,6-dichloro-1-b-D-ribofuranosyl-benzimidazole), TBB (4,5,6,7-tetrabromotriazole) and apigenin, as well as overexpression of a partial dominant negative mutant of CK2a, were shown to inhibit HIF-1 activity as measured by a reporter assay and through hypoxiainduced VEGF and aldolase expression. This does not occur at the stabilization process since they did not affect HIF-1a protein level. DNA-binding activity was also not inhibited. We conclude that CK2 is an important regulator of HIF-1 transcriptional activity but the mechanism of this regulation remains to be determined. Since HIF-1 plays a major role in tumor angiogenesis and since CK2 has been described to be overexpressed in tumor cells, this new pathway of regulation can be one more way for tumor cells to survive. ' 2005 Wiley-Liss, Inc.Key words: casein kinase 2; HIF-1; neoangiogenesis HIF-1 (hypoxia-inducible factor-1) is a key regulator of cell response to reduced oxygen level. In response to hypoxic conditions, HIF-1 increases the expression of downstream target genes such as erythropoietin (EPO), vascular endothelial growth factor (VEGF) and glycolytic enzymes (aldolase A, enolase-a) and mediates adaptation of cells to decreased oxygen level. 1 The role of HIF-1 in the regulation of tumor growth by hypoxia via the initiation of angiogenesis is certainly the best example of such an adaptive response. 2 Oncogene activation and tumor-suppressor inactivation result in deregulated cellular proliferation. However, most tumors grown larger than 1 mm 3 contain regions of low oxygen tension (hypoxia) due to an imbalance between oxygen supply and consumption. Formation of new blood vessels or ''neoangiogenesis'' is thus essential for further tumor growth. It is also important to allow tumor cell dissemination at distant sites, i.e., metastasis.Several studies using HIF-1 mutant cells have shown that HIF-1 has a profound effect on tumor biology. For example, tumors grown from HIF-1a-defective embryonic stem cells display abnormal vascularity and reduced growth rate. 3 Moreover, HIF-1 is upregulated in a broad r...

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Section: Discussionmentioning

confidence: 99%

Role for casein kinase 2 in the regulation of HIF‐1 activity

Mottet

Ruys

Demazy

et al. 2005

Intl Journal of Cancer

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“…Nevertheless, a few functions have been proposed : for example, an involvement in anti-apoptotic pathways [26] or in the cellular resistance to oxidative stress exploited by the combined superoxide dismutase activity and copperbinding capacity of PrP c [27,28]. Our results disclose another possible function of PrP, by showing that bPrP interacts with and up-regulates one of the most pleiotropic protein kinases, CK2, known to impinge on many proteins implicated in a variety of cell functions, in particular in signal transduction and gene expression pathways [1,8,29]. It is noteworthy that CK2 is also widely exploited by infectious agents, such as viruses and parasites, to perform the phosphorylation of proteins essential to their life cycle [29].…”

Section: Discussionmentioning

confidence: 63%

“…Protein kinase CK2 (an acronym derived from the misnomer ' casein kinase-2 ') is probably the most pleiotropic member of the huge family of protein kinases [1]. The long list of its substrates includes at least 200 proteins that share a phosphoacceptor site specified by multiple negatively charged amino acids [2].…”

Section: Introductionmentioning

confidence: 99%

Bovine prion protein as a modulator of protein kinase CK2

Meggio

Negro

Sarno

et al. 2000

Biochemical Journal

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On the basis of far-Western blot and plasmon resonance (BIAcore) experiments, we show here that recombinant bovine prion protein (bPrP) (25-242) strongly interacts with the catalytic α\αh subunits of protein kinase CK2 (also termed ' casein kinase 2 '). This association leads to increased phosphotransferase activity of CK2α, tested on calmodulin or specific peptides as substrate. We also show that bPrP counteracts the inhibition of calmodulin phosphorylation promoted by the regulatory β subunits of CK2. A truncated form of bPrP encompassing the Cterminal domain (residues 105-242) interacts with CK2 but does

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“…It has been reported that CKII activity increases when quiescent cells are stimulated to proliferate (Issinger, 1993;Allende and Allende, 1995;Pinna and Meggio, 1997). Studies performed using selective inhibitors also illustrate that CKII is required during various stages of cell cycle progression (Ford et al, 2000).…”

Section: Ckii Inhibitors Suppress Proliferation Of U87 Astroglioma Cellsmentioning

confidence: 97%

“…It exists as a constitutively active tetramer that contains two catalytic subunits, or ' (37-44 kDa), and two regulatory subunits (24-28 kDa) (Allende and Allende, 1995;Pinna and Meggio, 1997;Litchfield, 2002). The two catalytic subunits are highly homologous, but the ' subunit has a unique required role in spermatogenesis (Xu et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells

Ahn

Min²,

Bae³

et al. 2006

Exp Mol Med

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Elevated expression of protein casein kinase II (CKII) stimulated basal phospholipase D (PLD) activity as well as PMA-induced PLD activation in human U87 astroglioma cells. Moreover, CKII-selective inhibitor, emodin and apigenin suppressed PMA-induced PLD activation in a dose-dependent manner as well as basal PLD activity, suggesting the involvement of CKII in the activation of both PLD1 and PLD2. CKII was associated with PLD1 and PLD2 in co-transfection experiments. Furthermore, CKII induced serine/threonine phosphorylation of PLD2 in vivo, and the multiple regions of PLD2 were phosphorylated by CKII in vitro kinase assay using glutathione S-transferase-PLD2 fusion protein fragments. Elevated expression of CKII or PLD increased cell proliferation but pretreatment of cells with 1-butanol suppressed CKII-induced cell proliferation. These results suggest that CKII is involved in proliferation of U87 cells at least in part, through stimulation of PLD activity.

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Protein kinase CK2 (“casein kinase-2”) and its implication in cell division and proliferation

Cited by 317 publications

References 190 publications

Role for casein kinase 2 in the regulation of HIF‐1 activity

Role for casein kinase 2 in the regulation of HIF‐1 activity

Bovine prion protein as a modulator of protein kinase CK2

Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells

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