Serine phosphorylation-regulated ubiquitination and degradation of beta-catenin - PubMed (original) (raw)

. 1997 Oct 3;272(40):24735-8.

doi: 10.1074/jbc.272.40.24735.

Affiliations

• PMID: 9312064
• DOI: 10.1074/jbc.272.40.24735

Free article

Serine phosphorylation-regulated ubiquitination and degradation of beta-catenin

K Orford et al. J Biol Chem. 1997.

Free article

Abstract

Several lines of evidence suggest that accumulation of cytoplasmic beta-catenin transduces an oncogenic signal. We show that beta-catenin is ubiquitinated and degraded by the proteosome and that beta-catenin stability is regulated by a diacylglycerol-independent protein kinase C-like kinase activity, which is required for beta-catenin ubiquitination. We also define a six-amino acid sequence found in both beta-catenin and the NF-kappaB regulatory protein IkappaBalpha, which, upon phosphorylation, targets both proteins for ubiquitination. Mutation of a single serine within the ubiquitination targeting sequence prevents ubiquitination of beta-catenin. Mutations within the ubiquitination targeting sequence of beta-catenin may be oncogenic.

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