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. Y east two-hybrid assay, GST binding assay and immunoprecipitation demonstrat ed that delta-catenin interacted with a hydrophilic loop region in the endo proteolytic C-terminal fragment of PS1, but not with that of PS-2. These re sults suggest that PS1 and PS2 partly differ in function. PS1 loop fragment containing the pathogenic mutation retained the binding ability. We also f ound another armadillo-protein, p0071, interacted with PS1. (C) 1999 Lippin cott Williams & Wilkins.