Casein Kinase II: An attractive target for anti-cancer drug design

Hanif, Ismail Muhamad; Hanif, Ibrahim Muhammad; Shazib, Muhammad Ali; Ahmad, Kashif; Pervaiz, Shazib

doi:10.1016/j.biocel.2010.06.010

Cited by 55 publications

(45 citation statements)

References 29 publications

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“…It is likely that a relationship exists between Nop58 SUMOylation, ribosome biogenesis and cellular translation, and this might be revealed by investigating pre-rRNA processing in cells expressing mainly non-SUMOylatable Nop58. The phosphorylated S502 in Nop58 is situated within a consensus site for casein kinase II (CK2), 41,45 which is an ubiquitous serine/ threonine kinase with hundreds of cellular substrates, including the nucleolar proteins NOLC1 and B23. Both increased expression and increased activity of CK2 have been linked to human cancers.…”

Section: Nop58 and Sumo: What Are The Upstream Regulators?mentioning

confidence: 99%

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A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics

Westman

Lamond

2011

nucleus

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A role for SUMOylation in the biogenesis and/or function of Box C/D snoRNPs has been reported, mediated via SUMO2 conjugation to the core snoRNP protein, Nop58. A quantitative proteomics screen, based on SILAC (stable-isotope labeling by amino acids in cell culture) and mass spectrometry using extracts prepared from cultured mammalian cells expressing either 6His-SUMO1 or -SUMO2, revealed that the snoRNP-related proteins Nop58, Nhp2, DKC1 and NOLC1 are amongst the main SUMO-modified proteins in the nucleolus. SUMOylation of Nhp2 and endogenous Nop58 was confirmed using a combination of in vitro and cellbased assays and the modified lysines identified by site-directed mutagenesis. SUMOylation of Nop58 was found to be important for high-affinity Box C/D snoRNA binding and the localization of newly transcribed snoRNAs to the nucleolus. Here, these findings are reviewed and a model for understanding Nop58 SUMOylation in the context of Box C/D snoRNP biogenesis is presented. Given the essential role of snoRNPs in the modification of pre-ribosomal RNA, this work suggests that SUMO, snoRNPs and ribosome assembly, and thus cellular translation, growth and proliferation, may be linked via novel mechanisms which warrant further investigation.

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Section: Nop58 and Sumo: What Are The Upstream Regulators?mentioning

confidence: 99%

“…Both increased expression and increased activity of CK2 have been linked to human cancers. 45 It will be interesting to examine if CK2 activity regulates Nop58 phosphorylation What role might this K/E-rich region play in these otherwise unrelated proteins?…”

Section: Nop58 and Sumo: What Are The Upstream Regulators?mentioning

confidence: 99%

A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics

Westman

Lamond

2011

nucleus

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“…Identification of this component would improve our understanding of the complex regulatory network governed by activity of CK2 kinase. The other issue is linked with the potential use of inhibitors of CK2 in anticancer therapy (20,21) and concerns their efficacy as sensitizers to anticancer agents such as TRAIL. Although the schedule in which TBB treatment precedes administration of sTRAIL does not cause more cell death, it prevents elevated metabolic activity of the cancer cell that may overwhelm the apoptotic efficacy of the combination of TBB and TRAIL.…”

Section: Discussionmentioning

confidence: 99%

“…It also promotes cell survival acting on c-FLIP expression (16), increasing the level of survivin (17), and enhancing degradation of tumor suppressors: PML (18) and inositol hexakisphosphate kinase-2 (19). Due to general pro-survival effects of CK2 activity, its inhibitors are seriously considered as potential anticancer drugs (20,21). Their application seems especially promising in combination with other anticancer agents whose effective concentration might be reduced this way.…”

Section: Introductionmentioning

confidence: 99%

Time schedule-dependent effect of the CK2 inhibitor TBB on PC-3 human prostate cancer cell viability

Orzechowska

Kozłowska²,

Staroń³

et al. 2011

Oncol Rep

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Abstract. Inhibitors of CK2 kinase inhibit cell proliferation and induce apoptosis in numerous cancer cell lines. Due to these properties, they are considered potentially useful in anticancer therapy. In this study, we show that the exact effect of the specific CK2 inhibitor TBB on PC-3 human prostate cancer cell viability depends on the time schedule of administration: it was not observed when the treatment was directly followed by the viability assay but it appeared when the treatment and the assay were separated by a 24-h incubation without the inhibitor. Such a pattern was maintained when the TBB treatment was combined with either camptothecin or TRAIL. The time schedule-dependence of cell viability was not reflected by a similar dependence of induction of apoptosis. Despite this, the schedule in which a treatment with the CK2 inhibitor precedes that with an anticancer drug seems to be a good choice for a potential therapy against androgen-refractory prostate cancer.

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“…Casein Kinase II (CK2) is a ubiquitous kinase involved in intracellular signalling related to cellular growth and proliferation. It has been reported that deregulation of CK2 activity could be linked to the development of human cancers [18], and that its up-regulation has been described in glioblastomas [19]. Moreover, CK2 inhibition has been shown to have anti-tumor effect in human-glioblastoma xenografts [19,20].…”

Section: Introductionmentioning

confidence: 99%