1. Direct association of presenilin-1 with β-catenin
- Author
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Naomi Nihonmatsu, Akihiko Takashima, Kaori Yasutake, Ohoshi Murayama, Shoji Tanaka, James Palacino, Xiaoyan Sun, Miyuki Murayama, Benjamin Wolozin, and Toshiyuki Honda
- Subjects
Cytoplasm ,β-Catenin ,animal diseases ,Biophysics ,Gene Expression ,Endoplasmic Reticulum ,Transfection ,Biochemistry ,Presenilin ,Neuroblastoma ,Structure-Activity Relationship ,Alzheimer Disease ,Structural Biology ,mental disorders ,Gene expression ,Tumor Cells, Cultured ,Presenilin-1 ,Genetics ,Animals ,Humans ,Molecular Biology ,Immunosorbent Techniques ,beta Catenin ,Binding Sites ,COS cells ,Chemistry ,Endoplasmic reticulum ,Membrane Proteins ,Cell Biology ,Alzheimer's disease ,Peptide Fragments ,nervous system diseases ,Cell biology ,Cytoskeletal Proteins ,nervous system ,Catenin ,COS Cells ,Mutagenesis, Site-Directed ,Trans-Activators ,Signal transduction ,Glycogen synthase kinase 3β ,Signal Transduction - Abstract
Families bearing mutations in the presenilin-1 (PSI) gene develop Alzheimer's disease (AD). However, the mechanism through which PS1 causes AD is unclear. The co-immunoprecipitation with PS1 in transfected COS-7 cells indicates that PSI directly interacts with endogenous beta-catenin, and the interaction requires residues 322450 of PSI and 445-676 of beta-catenin. Both proteins are co-localized in the endoplasmic reticulum. Over-expression of PS1 reduces the level of cytoplasmic beta-catenin, and inhibits beta-catenin-T cell factor-regulated transcription. These results indicate that PSI plays a role as inhibitor of the beta-catenin signal, which may be connected with the AD dysfunction.
- Published
- 1998
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