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Direct association of presenilin‐1 with β‐catenin
Author(s) -
Murayama Miyuki,
Tanaka Shoji,
Palacino James,
Murayama Ohoshi,
Honda Toshiyuki,
Sun Xiaoyan,
Yasutake Kaori,
Nihonmatsu Naomi,
Wolozin Benjamin,
Takashima Akihiko
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00886-2
Subject(s) - presenilin , endoplasmic reticulum , catenin , immunoprecipitation , cytoplasm , transfection , microbiology and biotechnology , transcription factor , chemistry , endogeny , gene , biology , signal transduction , biochemistry , disease , alzheimer's disease , medicine , wnt signaling pathway
Families bearing mutations in the presenilin‐1 (PS1) 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 PS1 directly interacts with endogenous β‐catenin, and the interaction requires residues 322–450 of PS1 and 445–676 of β‐catenin. Both proteins are co‐localized in the endoplasmic reticulum. Over‐expression of PS1 reduces the level of cytoplasmic β‐catenin, and inhibits β‐catenin‐T cell factor‐regulated transcription. These results indicate that PS1 plays a role as inhibitor of the β‐catenin signal, which may be connected with the AD dysfunction.