Association of protein kinase CK2 with nuclear matrix: Influence of method of preparation of nuclear matrix

Tawfic, Sherif; Davis, Alan T.; Faust, Russell A.; Gapany, M.; Ahmed, Khalil

doi:10.1002/(sici)1097-4644(19970301)64:3<499::aid-jcb16>3.0.co;2-b

Cited by 21 publications

(10 citation statements)

References 16 publications

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“…After response to androgen or certain growth stimuli, protein kinase CK2 translocates from the cytosol to the nucleus, where it associates preferentially with the chromatin and the nuclear matrix (Guo et al 1999). Three different standard methods for nuclear matrix preparation were compared and quantitatively similar results were obtained for the stimulus-mediated modulation of nuclear matrix-associated CK2 (Tawfic et al 1997). Furthermore, androgen deprivation in rats led to a decreased activity and concentration of CK2 in the nuclear matrix (about 80%); but, after androgen administration in these deprived rats, CK2 activity and levels increased again in nuclear matrix fractions (110%; Tawfic and Ahmed 1994).…”

Section: Nuclear Matrixmentioning

confidence: 68%

Subcellular localization of protein kinase CK2

Faust

Montenarh

2000

Cell and Tissue Research

221

168

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More than 46 years ago, Burnett and Kennedy first described protein kinase CK2 (formerly known as casein kinase 2) in liver extracts. Since then, protein kinase CK2 has been investigated in many organisms from yeast to man. It is now well established that protein kinase CK2 is a pleiotropic and ubiquitous serine or threonine kinase, which is highly conserved during evolution. A great number of studies deal with substrates of CK2, but the fact that over 160 substrates exist is more confusing than elucidatory. The holoenzyme is composed of two regulatory beta-subunits and two catalytic alpha- or alpha'-subunits. There is now increasing evidence for individual functions of the subunits that are different from their functions in the holoenzyme. Furthermore, more and more studies describe interacting partners of the kinase that may be decisive in the regulation of this enzyme. A big step forward has been the determination of the crystal structure of the two subunits of protein kinase CK2. Now the interactions of the catalytic subunit of CK2 with ATP as well as GTP and the interaction between the regulatory subunits can be explained. However, cellular functions of protein kinase CK2 still remain unclear. In the present review we will focus our interest on the subcellular localization of protein kinase CK2. Protein kinase CK2 is found in many organisms and tissues and nearly every subcellular compartment. There is ample evidence that protein kinase CK2 has different functions in these compartments and that the subcellular localization of protein kinase CK2 is tightly regulated. Therefore studying the subcellular localization of protein kinase CK2 may be a key to its function.

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Section: Nuclear Matrixmentioning

confidence: 68%

Subcellular localization of protein kinase CK2

Faust

Montenarh

2000

Cell and Tissue Research

221

168

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“…The cells treated as above were utilized for isolation of the nuclear matrix. The nuclear matrix was prepared immediately from the washed cells using a previously described procedure referred to as Method C [Tawfic et al, 1997]. The recovery of protein in the nuclear matrix fraction was determined by a modified Coomassie staining procedure [Ahmed et al, 1996].…”

Section: Methodsmentioning

confidence: 99%

Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix

Wang

Davis

et al. 2002

J of Cellular Biochemistry

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Protein kinase CK2 is a ubiquitous protein serine/threonine kinase that is involved in cell growth and proliferation as well as suppression of apoptosis. Several studies have suggested that the kinase plays a role in cell cycle progression; however, changes in enzyme activity during phases of cell cycle have not been detected. Nuclear matrix is a key locus for CK2 signaling in the nucleus. We therefore examined CK2 signaling to the nuclear matrix in distinct phases of cell cycle by employing synchronized ALVA-41 prostate cancer cells. Removal of serum from the culture medium resulted in G0/G1 arrest, and a reduction in the nuclear matrix-associated CK2 activity which was rapidly reversed on addition of serum. Arresting the cells in G(0)/G(1) phase with hydroxyurea and subsequent release to S phase by serum gave similar results. Cells arrested in the G(2)/M phase by treatment with nocodazole demonstrated an extensive reduction in the nuclear matrix-associated CK2 which was reversed rapidly on addition of serum. Changes in the immunoreactive CK2 protein were concordant with the activity data reflecting a dynamic trafficking of the kinase in distinct phases of cell cycle. Under the same conditions, CK2 activity in total cellular lysate remained essentially unaltered. These results provide the first direct evidence of discrete modulations of CK2 in the nuclear matrix during the cell cycle progression. Inducible overexpression of CK2 in CHO cells yielded only a modest increase in CK2 activity even though a significant increase in expression was apparent at the level of CK2 alpha-specific message. Stably transfected ALVA-41 cells, however, did not show a significant change in CK2 levels despite increased expression at the message level. Not surprisingly, both types of the stably transfected cells failed to show any alteration in cell cycle progression. Distribution of the CK2 activity in the cytosolic versus nuclear matrix fractions in normal cells appears to be different from that in the cancer cells such that the ratio of nuclear matrix to cytosolic activity is much higher in the latter. Considering that nuclear matrix is central to several nuclear functions, this pattern of intracellular distribution of CK2 may have implications for its role in the oncogenic process. Published 2003 Wiley-Liss, Inc.

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“…Cell lysates and cell fractions (NM and cytoplasm) from rat ventral prostate tissue, and from cultured PC-3 and ALVA-41 prostate cancer cells were prepared as described previously (29). Ice-cold RIPA buffer was used for making total lysates whereas CSK buffer was employed for preparation of cell fractions, and in all cases Method C was used for preparation of cell fractions as detailed previously (29).…”

Section: Methodsmentioning

confidence: 99%

“…Ice-cold RIPA buffer was used for making total lysates whereas CSK buffer was employed for preparation of cell fractions, and in all cases Method C was used for preparation of cell fractions as detailed previously (29). Operationally, the nuclear matrix is known to contain the nucleolar component as was defined previously (24).…”

Section: Methodsmentioning

confidence: 99%

“…The suspension is centrifuged for 5 min at 600 × g, and the pellet (nuclear matrix fraction) is suspended by vortexing to obtain a uniform suspension in TMED + 0.2 M NaCl + Sigma’s protease inhibitor cocktail (x 0.01 of total volume) (TMED is 50 mM Tris-HCl pH 7.9 at room temp + 5 mM MgCl 2 + 1 mM EDTA + 0.5 mM DTT). Protein concentration was estimated as described previously (29). …”

Section: Methodsmentioning

confidence: 99%

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Protein B23/Nucleophosmin/Numatrin Nuclear Dynamics in Relation to Protein Kinase CK2 and Apoptotic Activity in Prostate Cells

et al. 2010

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Protein B23/nucleophosmin/numatrin3 is a key nucleolar/nuclear matrix associated protein required for cell growth related functions, such as rRNA synthesis. Protein kinase CK2 (formerly casein kinase 2, a protein ser/thr kinase signal that is involved in cell growth and cell death) mediates phosphorylation of B23 thereby influencing its functional activity. Here we have delineated the dynamics of B23 and its link to CK2 status in response to altered growth stimuli and induction of apoptosis in cultured prostate cells and in rat prostate cells in vivo. Our studies employing PC-3 and ALVA-41 prostate cancer cells demonstrated colocalization of CK2 and B23 in the nucleus. Further, CK2 and B23 underwent coordinate modulation in the nucleus related to their nucleocytoplasmic shuttling in response to induction of apoptotic activity in cells caused by downregulation of CK2 or by treatment with other apoptosis-inducing agents. These alterations in nuclear association of B23 occurred in the absence of a significant change in the level of cytoplasmic B23. Similar studies in the in vivo model of rat prostate epithelial cells subjected to androgen deprivation (that resulted in loss of nuclear CK2 and induction of apoptosis) demonstrated dynamic modulation of nuclear matrix associated B23 without a significant change in its cytoplasmic level. These changes were reversed by androgen-mediated growth response in the prostate. Our results suggest that CK2 mediated phosphorylation of B23 is essential for its retention in the nucleus, and that coordinate nuclear localization of B23 and CK2 is dynamically regulated in response to altered growth status in the cell.

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Association of protein kinase CK2 with nuclear matrix: Influence of method of preparation of nuclear matrix

Cited by 21 publications

References 16 publications

Subcellular localization of protein kinase CK2

Subcellular localization of protein kinase CK2

Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix

Protein B23/Nucleophosmin/Numatrin Nuclear Dynamics in Relation to Protein Kinase CK2 and Apoptotic Activity in Prostate Cells

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