Functional interaction of beta-catenin with the transcription factor LEF-1

Nature. 1996 Aug 15;382(6592):638-42. doi: 10.1038/382638a0.

Abstract

The cytoplasmic proteins beta-catenin of vertebrates and armadillo of Drosophila have two functions: they link the cadherin cell-adhesion molecules to the cytoskeleton, and they participate in the wnt/wingless signal pathway. Here we show, in a yeast two-hybrid screen, that the architectural transcription factor LEF-1 (for lymphoid enhancer-binding factor) interacts with beta-catenin. In mammalian cells, coexpressed LEF-1 and beta-catenin form a complex that is localized to the nucleus and can be detected by immunoprecipitation. Moreover, LEF-1 and beta-catenin form a ternary complex with DNA that splays an altered DNA bend. Microinjection of LEF-1 into XenoPus embryos induces axis duplication, which is augmented by interaction with beta-catenin. Thus beta-catenin regulates gene expression by direct interaction with transcription factors such as LEF-1, providing a molecular mechanism for the transmission of signals, from cell-adhesion components or wnt protein to the nucleus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cadherins / metabolism*
  • Cell Line
  • Cell Nucleus / metabolism
  • Cloning, Molecular
  • Cytoskeletal Proteins / metabolism*
  • DNA / metabolism
  • DNA-Binding Proteins / metabolism*
  • Drosophila
  • Escherichia coli
  • Lymphoid Enhancer-Binding Factor 1
  • Nucleic Acid Conformation
  • Protein Binding
  • RNA, Messenger / genetics
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae / genetics
  • Trans-Activators*
  • Transcription Factors / metabolism*
  • Xenopus
  • Xenopus Proteins
  • beta Catenin

Substances

  • CTNNB1 protein, Xenopus
  • Cadherins
  • Cytoskeletal Proteins
  • DNA-Binding Proteins
  • Lymphoid Enhancer-Binding Factor 1
  • RNA, Messenger
  • Recombinant Proteins
  • Trans-Activators
  • Transcription Factors
  • Xenopus Proteins
  • beta Catenin
  • DNA