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doi: 10.1242/10.1242/jcs.00074

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Protein kinase CK2: a challenge to canons

Department of Biological Chemistry, University of Padova, V.le G. Colombo, 3 35121 Padova, Italy and Venetian Institute for Molecular Medicine (VIMM), Via Orus 2, 23129 Padova, Italy

View larger version (26K): [in a new window]   Fig. 1. The paradox of CK2 constitutive activity. Unlike PKA and CDKs, CK2 does not undergo drastic changes in catalytic activity upon association between catalytic and regulatory subunits. However the phosphorylation of some protein substrates can be deeply altered in this way.

View larger version (26K): [in a new window]   Fig. 2. Hypothesized dual role of CK2 in the Wnt signaling pathway. Direct phosphorylation by CK2 prevents ß-catenin degradation, counteracting the effect of GSK3 phosphorylation within the negative regulatory complex (Son et al., 2000). On the other hand, CK2, by phosphorylating the E2 ubiquitin-conjugating enzyme UBC3, promotes its binding to the proteasome receptor ß-TrCP, ultimately assisting the degradation of ß-catenin (Semplici et al., 2002).

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