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.
Tanahashi
H
H
Division of Demyelinating Disease and Aging, National Institute of Neuroscience, Kodaira, Tokyo, Japan.
Tabira
T
T
D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D051186:Armadillo Domain Proteins; D019556:COS Cells; D051177:Catenins; D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D018076:DNA, Complementary / Q000235:genetics; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D010750:Phosphoproteins; D051191:Plakophilins; D011233:Precipitin Tests; D053764:Presenilin-1; D053766:Presenilin-2; D013379:Substrate Specificity / Q000502:physiology; D000095002:Delta Catenin
D051186:Armadillo Domain Proteins; D051177:Catenins; D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary; D008565:Membrane Proteins; C105677:PKP4 protein, human; C508853:PSEN1 protein, human; C508861:PSEN2 protein, human; D010446:Peptide Fragments; D010750:Phosphoproteins; D051191:Plakophilins; D053764:Presenilin-1; D053766:Presenilin-2; D000095002:Delta Catenin