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

Neuroreport. 1999 Feb 25;10(3):563-8. doi: 10.1097/00001756-199902250-00022.

Abstract

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.

MeSH terms

  • Amino Acid Sequence / genetics
  • Animals
  • Armadillo Domain Proteins
  • COS Cells
  • Catenins
  • Cell Adhesion Molecules
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / isolation & purification*
  • Cytoskeletal Proteins / metabolism*
  • DNA, Complementary / genetics
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Peptide Fragments / metabolism
  • Phosphoproteins
  • Plakophilins
  • Precipitin Tests
  • Presenilin-1
  • Presenilin-2
  • Substrate Specificity / physiology

Substances

  • Armadillo Domain Proteins
  • Catenins
  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • DNA, Complementary
  • Membrane Proteins
  • PKP4 protein, human
  • PSEN1 protein, human
  • PSEN2 protein, human
  • Peptide Fragments
  • Phosphoproteins
  • Plakophilins
  • Presenilin-1
  • Presenilin-2
  • delta catenin

Associated data

  • GENBANK/AB013805