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Molecular and Cellular Biochemistry

, Volume 316, Issue 1–2, pp 115–126 | Cite as

Ability of CK2β to selectively regulate cellular protein kinases

  • Birgitte B. Olsen
  • Barbara Guerra
Article

Abstract

The Wee1 protein kinase plays a prominent role in keeping cyclin dependent kinase 1 (CDK1) inactive during the G2 phase of the cell cycle. At the onset of mitosis, Wee1 is ubiquitinated by the E3 ubiquitin ligase SCFβ-TrCP and subsequently degraded by the proteasome machinery. Previously, it has been reported that although Wee1 lacks the conserved binding motif recognised by β-TrCP, the CDK-catalysed phosphorylation of Wee1 at Ser123 creates a phosphodegron and primes phosphorylation of two other protein kinases, polo-like kinase 1 (PLK1) and protein kinase CK2, which create two additional phosphodegrons recognised by β-TrCP. These events contribute to destabilise Wee1 at the onset of mitosis (Watanabe et al. Proc Natl Acad Sci USA 101:4419–4424, 2004). We show here that in addition to the ability of CK2 to phosphorylate Wee1 as reported earlier, the regulatory β-subunit of protein kinase CK2 can interact with Wee1 in high molecular mass complexes. Indirect immunofluorescence microscopy revealled subcellular co-localisation of CK2β and Wee1 in the nucleus. Moreover, in vitro phosphorylation assays showed that CK2β indirectly up-regulates the activity of CDK1 with respect to histone H1 phosphorylation by inhibiting Wee1 kinase. These findings support the view that CK2β regulates various intracellular processes by modulating the activity of protein kinases that are distinct from CK2 and that protein kinase CK2 plays an important role in events related to the regulation of cell cycle progression as a tetrameric enzyme but also through the individual subunits.

Keywords

Protein kinase CK2 Wee1 Phosphorylation Protein interaction 

Notes

Acknowledgments

We thank Dr. O.-G. Issinger for critically reading the manuscript and Tina Holm for excellent technical assistance. This work was supported by a bequest for cancer research from Karen Marie Maaløe, Odense, Denmark and the Novo Nordisk Foundation, grant no. 5373 to B.G.

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Copyright information

© Springer Science+Business Media, LLC. 2008

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyUniversity of Southern DenmarkOdenseDenmark

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