PMID:12432063

Citation	Bek, S and Kemler, R (2002) Protein kinase CKII regulates the interaction of beta-catenin with alpha-catenin and its protein stability. J. Cell. Sci. 115:4743-53
Abstract	beta-Catenin is a multi-functional cellular component and a substrate for several protein kinases. Here we investigated the interaction of protein kinase CKII (casein kinase II) and beta-catenin. We show that CKII phosphorylates the N-terminal region of beta-catenin and we identified Ser29, Thr102, and Thr112 as substrates for the enzyme. We provide evidence that CKII regulates the cytoplasmic stability of beta-catenin and acts synergistically with GSK-3beta in the multi-protein complex that controls the degradation of beta-catenin. In comparing wild-type and Ser/Thr-mutant beta-catenin, a decreased affinity of the mutant protein to alpha-catenin was observed. Moreover, kinase assays in vitro demonstrate a CKII-dependent increase in the binding of wild-type beta-catenin with alpha-catenin. In line with that, cells expressing Ser/Thr-mutant beta-catenin exhibit an increased migratory potential, which correlates with an enhanced cytosolic localization and a reduced association with the cytoskeleton of the mutant protein. From these results we conclude that CKII regulates the function of beta-catenin in the cadherin adhesion complex as well as its cytoplasmic stability.
Links	PubMed
Keywords	Amino Acid Sequence; Animals; Base Sequence; Casein Kinase II; Cell Line; Cytoplasm/metabolism; Cytoskeletal Proteins/chemistry; Cytoskeletal Proteins/metabolism; DNA Primers; Humans; Immunohistochemistry; Mice; Molecular Sequence Data; Phosphorylation; Protein Binding; Protein-Serine-Threonine Kinases/metabolism; Sequence Homology, Amino Acid; Trans-Activators/chemistry; Trans-Activators/metabolism; alpha Catenin; beta Catenin
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