Elevated protein kinase CK2 activity in chromatin of head and neck tumors: association with malignant transformation

Faust, Russell A.; Gapany, M.; Tristani, Payam; Davis, Alan T.; Adams, George L.; Ahmed, Khalil

doi:10.1016/0304-3835(96)04110-9

Cited by 146 publications

(131 citation statements)

References 13 publications

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“…Experimental transgenic mouse models of neoplasia in which altered CK2 signal served as a double transgene have provided significant support to this notion (e.g., Kelliher et al, 1996;Xu et al, 1999). The presence of elevated CK2 in cancer appears to correlate with the pathological status of the cancer and may serve as a prognostic marker (Yenice et al, 1994;Gapany et al, 1995;Faust et al, 1996;Faust et al, 1999;Piazza et al, 2006;Laramas et al, 2007). Although CK2 is present ubiquitously in all cells, it is noteworthy that its distribution in the normal versus cancer cells is distinct.…”

Section: Ck2 and Cancermentioning

confidence: 98%

Protein kinase CK2 – A key suppressor of apoptosis

Ahmad

Wang

Unger

et al. 2008

Advances in Enzyme Regulation

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233

188

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Section: Ck2 and Cancermentioning

confidence: 98%

Protein kinase CK2 – A key suppressor of apoptosis

Ahmad

Wang

Unger

et al. 2008

Advances in Enzyme Regulation

Self Cite

233

188

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“…It binds and phosphorylates TFIIIB in both yeast and mammals, and can increase pol III transcription dramatically by facilitating assembly of the initiation complex (Hockman and Schultz, 1996;Schultz, 1997, 2001;Johnston et al, 2002). It induces lymphomas in transgenic mice and is hyperactive in some human malignancies (Faust et al, 1996;Munstermann et al, 1990;Notterman et al, 2001;Seldin and Leder, 1995). Elevated pol III output may be driven by CK2 in such circumstances, although this has yet to be tested experimentally.…”

Section: Direct Activation Of Tfiiibmentioning

confidence: 99%

RNA polymerase III transcription and cancer

2004

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RNA polymerase (pol) III synthesizes a range of essential products, including tRNA, 5S rRNA and 7SL RNA, which are required for protein synthesis and trafficking. High rates of pol III transcription are necessary for cells to sustain growth. A wide range of transformed and tumour cell types have been shown to express elevated levels of pol III products. This review will summarize what is known about the mechanisms responsible for this deregulation. Some transforming agents have been shown to stimulate expression of the pol III-specific transcription factors TFIIIB or TFIIIC2. In addition, TFIIIB is bound and activated by several oncogenic proteins, including cMyc. Conversely, TFIIIB interacts in healthy cells with the tumour suppressors RB and p53. Indeed, the ability to limit pol III transcription through TFIIIB may contribute to their growth-suppression capacities. The function of p53 and/or RB is compromised in most if not all transformed cells; the resultant derepression of TFIIIB may provide an almost universal route to deregulate pol III transcription in cancers. In addition to effects on protein synthesis and growth, there is a precedent for a pol III product having oncogenic activity.

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“…Dysregulated CK2 protein expression was first reported in a bovine pseudo-leukemia caused by a protozoan parasite (ole-MoiYoi et al, 1992). A series of additional papers have documented its upregulation in many human cancers including leukemias (Daya-Makin et al, 1994;Faust et al, 1996;Gapany et al, 1995), and solid tumors (Faust et al, 1996(Faust et al, , 1999Munstermann et al, 1990) including breast cancer (Landesman-Bollag et al, 2001). We have utilized transgenic mice to demonstrate that dysregulated expression of CK2 contributes to lymphocyte transformation (Seldin and Leder, 1995).…”

Section: Introductionmentioning

confidence: 95%

Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis

2002

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Protein kinase CK2 (formerly casein kinase II) is frequently upregulated in human cancers, and transgenic expression of CK2a in lymphocytes is oncogenic. Lymphomagenesis is dramatically acclerated by coexpression of a c-myc transgene, suggestive of a synergistic interaction between the kinase and the transcription factor. Since c-myc can be phosphorylated by CK2, we hypothesized that the synergy between CK2 and c-myc might be due to a functional interaction of the two molecules. Pharmacologic inhibition of CK2 activity in cell lines established from CK2a transgenic T cell lymphomas reduces their proliferation and concomitantly with this, the steady state levels of c-myc protein decline. This is caused by acclerated c-myc protein turnover, which occurs in a proteasome-dependent manner. Transfection of cells with sense or anti-sense CK2 constructs modulates c-myc protein levels in concert with the alteration in CK2 activity, validating the findings obtained using the kinase inhibitors. Thus, CK2 is a critical regulator of c-myc protein stability and of the proliferation of these T cell lymphomas.

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Elevated protein kinase CK2 activity in chromatin of head and neck tumors: association with malignant transformation

Cited by 146 publications

References 13 publications

Protein kinase CK2 – A key suppressor of apoptosis

Protein kinase CK2 – A key suppressor of apoptosis

RNA polymerase III transcription and cancer

Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis

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