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.
Mesh Terms:
Amino Acid Sequence, Animals, Armadillo Domain Proteins, COS Cells, 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
Amino Acid Sequence, Animals, Armadillo Domain Proteins, COS Cells, 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
Neuroreport
Date: Feb. 25, 1999
PubMed ID: 10208590
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