Characterization of a B-Catenin-Associated Kinase.
Abstract
Several lines of evidence suggest that accumulation of cytoplasmic Beta-catenin transduces an oncogenic signal. We show that Beta-cantenin is ubiquitinated and degraded by the proteosome and that Beta-cantenin 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-kB regulatory protein IkappaBalpha which, upon phosphorylation, targets both proteins for ubiqultination. Mutation of a single serine within the ubiquitin targeting sequence (UTS) prevents ubiquitination of Beta-catenin. Mutations within the UTS of Beta-catenin may be oncogenic.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 1998
- Accession Number
- ADA375192
Entities
People
- Stephen W. Byers
Organizations
- Georgetown University