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
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Amino Acid Sequence / genetics
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Animals
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Armadillo Domain Proteins
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COS Cells
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Catenins
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Cell Adhesion Molecules
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / isolation & purification*
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Cytoskeletal Proteins / metabolism*
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DNA, Complementary / genetics
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Delta Catenin
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Humans
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Peptide Fragments / metabolism
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Phosphoproteins
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Plakophilins
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Precipitin Tests
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Presenilin-1
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Presenilin-2
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Substrate Specificity / physiology
Substances
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Armadillo Domain Proteins
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Catenins
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Cell Adhesion Molecules
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Cytoskeletal Proteins
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DNA, Complementary
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Membrane Proteins
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PKP4 protein, human
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PSEN1 protein, human
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PSEN2 protein, human
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Peptide Fragments
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Phosphoproteins
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Plakophilins
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Presenilin-1
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Presenilin-2
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Delta Catenin