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A Molecular and Cellular View of Protein Kinase CK2 pp 213–222Cite as

Expression and regulation of protein kinase CK2 during the cell cycle

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Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 27))

Abstract

There are indications from genetic, biochemical and cell biological studies that protein kinase CK2 (formerly casein kinase II) has a variety of functions at different stages in the cell cycle. To further characterize CK2 and its potential roles during cell cycle progression, one of the objectives of this study was to systematically examine the expression of all three subunits of CK2 at different stages in the cell cycle. To achieve this objective, we examined levels of CK2α, CK2α′ and CK2β on immunoblots as well as CK2 activity in samples prepared from: (i) elutriated populations of MANCA (Burkitt lymphoma) cells, (ii) serum-stimulated GL30-92/R (primary human fibroblasts) cells and (iii) drug-arrested chicken bursal lymphoma BK3 A cells. On immunoblots, we observed a significant and co-ordinate increase in the expression of CK2α and CK2α′ following serum stimulation of quiescent human fibroblasts. By comparison, no major fluctuations in CK2 activity were detected during any other stages during the cell cycle. Furthermore, we did not observe any dramatic differences between the relative levels of CK2α to CK2α′ during different stages in the cell cycle. However, we observed a significant increase in the amount of CK2β relative to CK2α in cells arrested with nocodazole. We also examined the activity of CK2 in extracts or in immunoprecipitates prepared from drug-arrested cells. Of particular interest is the observation that the activity of CK2 is not changed in nocodazole-arrested cells. Since CK2 is maximally phosphorylated in these cells, this result suggests that the phosphorylation of CK2 by p34cdc2 does not affect the catalytic activity of CK2. However, the activity of CK2 was increased by incubation with p34cdc2 in vitro. Since this activation was independent of ATP we speculate that p34cdc2 may have an associated factor that stimulates CK2 activity. Collectively, the observations that relative levels of CK2β increase in mitotic cells, that CK2α and CK2β are phosphorylated in mitotic cells and that p34cdc2 affects CK2 activity in vitro suggest that CK2 does have regulatory functions associated with cell division. (Mol Cell Biochem 191: 213–222, 1999)

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Author information

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Manitoba, Winnipeg, Manitoba, Canada

    Denis G. Bosc

  2. Institut für Molekularbiologie, Medizinische Hochschule Hannover, Hannover, Germany

    Bernhard Lüscher

  3. Department of Biochemistry, Health Sciences Centre, University of Western Ontario, London, Ontario, Canada

    David W. Litchfield

Authors
  1. Denis G. Bosc
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  2. Bernhard Lüscher
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  3. David W. Litchfield
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Editor information

Editors and Affiliations

  1. Cellular and Molecular Biochemistry, Research Laboratory (151) V.A. Medical Centre, One Veterans Drive, Minneapolis, MN, 55417, USA

    Khalil Ahmed

  2. Biokemisk Institut, Odense Universitet, Campusvej 55, DK-5230, Odense M, Denmark

    O. G. Issinger

  3. Laboratoire de Biochemie des Regulations Cellulaires Endocrines, INSERM U244 DBMS, CEA Grenoble, 17 rue des Martyrs, F-38054, Grenoble Cedex 9, France

    E. Chambaz

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© 1999 Springer Science+Business Media Dordrecht

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Bosc, D.G., Lüscher, B., Litchfield, D.W. (1999). Expression and regulation of protein kinase CK2 during the cell cycle. In: Ahmed, K., Issinger, O.G., Chambaz, E. (eds) A Molecular and Cellular View of Protein Kinase CK2. Developments in Molecular and Cellular Biochemistry, vol 27. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8624-5_26

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  • DOI: https://doi.org/10.1007/978-1-4419-8624-5_26

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4648-7

  • Online ISBN: 978-1-4419-8624-5

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