Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Short Report
  • Published:

The ‘regulatory’ β-subunit of protein kinase CK2 negatively influences p53-mediated allosteric effects on Chk2 activation

Oncogene volume 24, pages 6194–6200 (2005)Cite this article

Abstract

The ‘regulatory’β-subunit of protein kinase CK2 has previously been shown to interact with protein kinases such as A-Raf, c-Mos, Lyn and Chk1 in addition to the catalytic subunit of CK2. Sequence alignments suggest that these interactions have a structural basis, and hence other protein kinases harboring corresponding sequences may be potential interaction partners for CK2β. We show here that Chk2 specifically interacts with CK2β in vitro and in cultured cells, and that activation of Chk2 leads to a reduction of this interaction. Additionally, we show that the presence of the CK2β-subunit significantly reduces the Chk2-catalysed phosphorylation of p53 in vitro. These findings support the notion that CK2β can act as a general modulator of remote docking sites in protein kinase – substrate interactions.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Figure 1
Figure 2
Figure 3

Similar content being viewed by others

References

  • Ahmed K, Gerber DA and Cochet C . (2002). Trends Cell Biol., 12, 226–230.

  • Ahn J, Urist M and Prives C . (2004). DNA Repair, 3, 1039–1047.

  • Appel K, Wagner P, Boldyreff B, Issinger OG and Montenarh M . (1995). Oncogene, 11, 1971–1978.

  • Bartek J, Falck J and Lukas J . (2001). Nat. Rev. Mol. Cell Biol., 2, 877–886.

  • Bartek J and Lukas J . (2003). Cancer Cell, 3, 421–429.

  • Bell S, Hansen S and Buchner J . (2002). Biophys. Chem., 96, 243–257.

  • Biondi RM and Nebreda AR . (2003). Biochem. J., 372, 1–13.

  • Boehden GS, Restle A, Marschalek R, Stocking C and Wiesmüller L . (2004). Carcinogenesis, 25, 1305–1313.

  • Boldyreff B and Issinger OG . (1997). FEBS Lett., 403, 197–199.

  • Boldyreff B, Meggio F, Pinna LA and Issinger OG . (1993). Biochemistry, 32, 12672–12677.

  • Cardenas ME, Dang Q, Glover CV and Gasser SM . (1992). EMBO J., 11, 1785–1796.

  • Chen M and Cooper JA . (1997). Proc. Natl. Acad. Sci. USA, 94, 9136–9140.

  • Chen M, Li D, Krebs ED and Cooper JA . (1997). Mol. Cell. Biol., 17, 1904–1912.

  • Craig A, Scott M, Burch L, Smith G, Ball K and Hupp T . (2003). EMBO Rep., 4, 787–792.

  • Daum JR and Gorbsky GJ . (1998). J. Biol. Chem., 273, 30622–30629.

  • Escargueil AE, Plisov SY, Filhol O, Cochet C and Larsen AK . (2000). J. Biol. Chem., 275, 34710–34718.

  • Farmer G, Bargonetti J, Zhu H, Friedman P, Prywes R and Prives C . (1992). Nature, 358, 83–86.

  • Ford HL, Landesmann-Bollag E, Dacwag CS, Stukenberg PT, Pardee AB and Seldin DC . (2000). J. Biol. Chem., 275, 22245–22254.

  • Goldberg Y . (1999). Biochem. Pharmacol., 57, 321–328.

  • Götz C, Scholtes P, Prowald A, Schuster N, Nastainczyk W and Montenarh M . (1999). Mol. Cell Biochem., 191, 111–120.

  • Grankowski N, Boldyreff B and Issinger OG . (1991). Eur. J. Biochem, 198, 25–30.

  • Guerra B, Götz C, Wagner P, Montenarh M and Issinger OG . (1997). Oncogene, 14, 2683–2688.

  • Guerra B and Issinger OG . (1999). Electrophoresis, 20, 391–408.

  • Guerra B, Issinger OG and Wang JY . (2003). Oncogene, 22, 4933–4942.

  • Guerra B, Siemer S, Boldyreff B and Issinger OG . (1999). FEBS Lett., 462, 353–357.

  • Huse M and Kuriyan J . (2002). Cell, 109, 275–282.

  • Kern SE, Kinzler KW, Bruskin A, Jarosz D, Friedman P, Prives C and Vogelstein B . (1991). Science, 252, 1708–1711.

  • Korn I, Gutkind S, Srinivasan N, Blundell TL, Allende CC and Allende JE . (1999). Mol. Cell Biochem., 191, 75–83.

  • Kusk M, Ahmed R, Thomsen B, Bendixen C, Issinger OG and Boldyreff B . (1999). Mol. Cell. Biochem., 191, 51–58.

  • Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD and Sanderson CM . (2004). Genomics, 83, 153–167.

  • Litchfield DW . (2003). Biochem. J., 369, 1–15.

  • Lorenz P, Pepperkok R and Pyerin W . (1994). Cell. Mol. Biol. Res., 40, 519–527.

  • Luciani MG, Hutchins JR, Zheleva D and Hupp TR . (2000). J. Mol. Biol., 300, 503–518.

  • Meggio F, Boldyreff B, Marin O, Marchiori F, Perich JW, Issinger OG and Pinna LA . (1992). Eur. J. Biochem., 205, 939–945.

  • Niefind K, Guerra B, Ermakowa I and Issinger OG . (2001). EMBO J., 20, 5320–5331.

  • O'Neill T, Giarratani L, Chen P, Iyer L, Lee CH, Bobiak M, Kanai F, Zhou BB, Chung JH and Rathbun GA . (2002). J. Biol. Chem., 277, 16102–16115.

  • Pepperkok R, Lorenz P, Ansorge W and Pyerin W . (1994). J. Biol. Chem., 269, 6986–6991.

  • Povirk LF . (1996). Mutat. Res., 355, 71–89.

  • Prowald A, Schuster N and Montenarh M . (1997). FEBS Lett., 408, 99–104.

  • Schuster N, Götz C, Faust M, Schneider E, Prowald A, Jungbluth A and Montenarh M . (2001). J. Cell. Biochem., 81, 172–183.

  • Schwindling SL, Noll A, Montenarh M and Götz C . (2004). Oncogene, 23, 4155–4165.

  • Seo GJ, Kim SE, Lee YM, Lee JW, Hahn MJ and Kim ST . (2003). Biochem. Biophys. Res. Commun., 304, 339–343.

  • Soussi T and May P . (1996). J. Mol. Biol., 260, 623–637.

  • Stalter G, Siemer S, Becht E, Ziegler M, Remberger K and Issinger OG . (1994). Biochem. Biophys. Res. Commun., 202, 141–147.

  • Stigare J, Buddelmeijer N, Pigon A and Egyhazi E . (1993). Mol. Cell. Biochem., 129, 77–85.

  • Theis-Febvre N, Filhol O, Froment C, Cazales M, Cochet C, Monsarrat B, Ducommmun B and Baldin V . (2003). Oncogene, 22, 220–232.

  • Toczyski DP, Galgoczy DJ and Hartwell LH . (1997). Cell, 90, 1097–1106.

Download references

Acknowledgements

We thank Hans H Jensen for technical support and Dr B Boldyreff (KinaseDetect) for purification of p53 and Chk2. This work was supported by the Danish Cancer Society, Grant No. 002521109210 and the Danish Research Council, Grant No. 21-01-0511 to O-G Issinger, plus the Deutsche Forschungsgemeinschaft, Grants Wi 1376/3-1 to L Wiesmüller and NI 643/1-2 to K Niefind.

Author information

Authors and Affiliations

  1. Institut for Biokemi og Molekylær Biologi, Syddansk Universitet, Odense, Denmark

    Marina Bjørling-Poulsen & Olaf-Georg Issinger

  2. Gynäkologische Onkologie, Universitätsfrauenklinik, Universität Ulm, Ulm, Germany

    Simone Siehler & Lisa Wiesmüller

  3. Biomedical Research Centre, Ninewells Hospital and Medical School, University of Dundee, Scotland, UK

    David Meek

  4. Institut für Biochemie, Universität zu Köln, Köln, Germany

    Karsten Niefind

Authors
  1. Marina Bjørling-Poulsen
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Simone Siehler
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Lisa Wiesmüller
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. David Meek
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Karsten Niefind
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Olaf-Georg Issinger
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Olaf-Georg Issinger.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Bjørling-Poulsen, M., Siehler, S., Wiesmüller, L. et al. The ‘regulatory’ β-subunit of protein kinase CK2 negatively influences p53-mediated allosteric effects on Chk2 activation. Oncogene 24, 6194–6200 (2005). https://doi.org/10.1038/sj.onc.1208762

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/sj.onc.1208762

Keywords

This article is cited by

Search

Advanced search

Quick links