The C-terminal domain of armadillo binds to hypophosphorylated teashirt to modulate wingless signalling in Drosophila

EMBO J. 1999 Apr 15;18(8):2208-17. doi: 10.1093/emboj/18.8.2208.

Abstract

Wnt signalling is a key pathway for tissue patterning during animal development. In Drosophila, the Wnt protein Wingless acts to stabilize Armadillo inside cells where it binds to at least two DNA-binding factors which regulate specific target genes. One Armadillo-binding protein in Drosophila is the zinc finger protein Teashirt. Here we show that Wingless signalling promotes the phosphorylation and the nuclear accumulation of Teashirt. This process requires the binding of Teashirt to the C-terminal end of Armadillo. Finally, we present evidence that the serine/threonine kinase Shaggy is associated with Teashirt in a complex. We discuss these results with respect to current models of Armadillo/beta-catenin action for the transmission of the Wingless/Wnt pathway.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Armadillo Domain Proteins
  • Drosophila / genetics
  • Drosophila / metabolism*
  • Drosophila Proteins*
  • Insect Proteins / chemistry
  • Insect Proteins / metabolism*
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Binding
  • Proto-Oncogene Proteins / metabolism*
  • Repressor Proteins*
  • Sequence Homology, Amino Acid
  • Signal Transduction*
  • Subcellular Fractions / metabolism
  • Trans-Activators*
  • Transcription Factors / metabolism*
  • Wnt1 Protein

Substances

  • ARM protein, Drosophila
  • Armadillo Domain Proteins
  • Drosophila Proteins
  • Insect Proteins
  • Proto-Oncogene Proteins
  • Repressor Proteins
  • Trans-Activators
  • Transcription Factors
  • Wnt1 Protein
  • wg protein, Drosophila
  • tsh protein, Drosophila