Work

Serine Phosphorylation-regulated Ubiquitination and Degradation of β-Catenin

Year: 1997

Type: 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.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.272.40.24735

Authors: Keith Orford, Caroline Crockett, Jane P. Jensen, Allan M. Weissman, Stephen W. Byers

Institutions: Georgetown University Medical Center, Georgetown Lombardi Comprehensive Cancer Center, National Institutes of Health, National Cancer Institute

Language: English

Topic: Wnt/β-catenin signaling in development and cancer

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430