Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A.
Journal Article (Journal Article)
Dysregulation of Wnt-beta-catenin signaling disrupts axis formation in vertebrate embryos and underlies multiple human malignancies. The adenomatous polyposis coli (APC) protein, axin, and glycogen synthase kinase 3beta form a Wnt-regulated signaling complex that mediates the phosphorylation-dependent degradation of beta-catenin. A protein phosphatase 2A (PP2A) regulatory subunit, B56, interacted with APC in the yeast two-hybrid system. Expression of B56 reduced the abundance of beta-catenin and inhibited transcription of beta-catenin target genes in mammalian cells and Xenopus embryo explants. The B56-dependent decrease in beta-catenin was blocked by oncogenic mutations in beta-catenin or APC, and by proteasome inhibitors. B56 may direct PP2A to dephosphorylate specific components of the APC-dependent signaling complex and thereby inhibit Wnt signaling.
Full Text
Duke Authors
Cited Authors
- Seeling, JM; Miller, JR; Gil, R; Moon, RT; White, R; Virshup, DM
Published Date
- March 26, 1999
Published In
Volume / Issue
- 283 / 5410
Start / End Page
- 2089 - 2091
PubMed ID
- 10092233
International Standard Serial Number (ISSN)
- 0036-8075
Digital Object Identifier (DOI)
- 10.1126/science.283.5410.2089
Language
- eng
Conference Location
- United States