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Isolation of human delta-catenin and its binding specificity with presenilin 1.

We screened proteins for interaction with presenilin (PS) 1, and cloned the full-length cDNA of human delta-catenin, which encoded 1225 amino acids. Yeast two-hybrid assay, GST binding assay and immunoprecipitation demonstrated that delta-catenin interacted with a hydrophilic loop region in the endoproteolytic C-terminal fragment of PS1, but not with that of PS-2. These results suggest that PS1 and PS2 partly differ in function. PS1 loop fragment containing the pathogenic mutation retained the binding ability. We also found another armadillo-protein, p0071, interacted with PS1.

Pubmed ID: 10208590


  • Tanahashi H
  • Tabira T



Publication Data

February 25, 1999

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Armadillo Domain Proteins
  • COS Cells
  • Catenins
  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • DNA, Complementary
  • Humans
  • Membrane Proteins
  • Molecular Sequence Data
  • Peptide Fragments
  • Phosphoproteins
  • Plakophilins
  • Precipitin Tests
  • Presenilin-1
  • Presenilin-2
  • Substrate Specificity