Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A.

Published

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

Pubmed Central 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