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

Marina Bjørling-Poulsen, Simone Siehler, Lisa Wiesmüller, David Meek, Karsten Niefind, Olaf-Georg Issinger

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    15 Citations (Scopus)

    Abstract

    The 'regulatory' beta-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 CK2beta. We show here that Chk2 specifically interacts with CK2beta 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 CK2beta-subunit significantly reduces the Chk2-catalysed phosphorylation of p53 in vitro. These findings support the notion that CK2beta can act as a general modulator of remote docking sites in protein kinase--substrate interactions.
    Original languageEnglish
    Pages (from-to)6194-6200
    Number of pages7
    JournalOncogene
    Volume24
    Issue number40
    DOIs
    Publication statusPublished - 8 Sep 2005

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    Bjørling-Poulsen, M., Siehler, S., Wiesmüller, L., Meek, D., Niefind, K., & Issinger, O-G. (2005). The 'regulatory' β-subunit of protein kinase CK2 negatively influences p53-mediated allosteric effects on Chk2 activation. Oncogene, 24(40), 6194-6200. https://doi.org/10.1038/sj.onc.1208762