The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein

被引：47

作者：

Chen, TY ^{[1
]}

Liu, PH ^{[1
]}

Ruan, CT ^{[1
]}

Chiu, L ^{[1
]}

Kung, FL ^{[1
]}

机构：

[1] Natl Taiwan Univ, Sch Pharm, Taipei 10051, Taiwan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 342卷 / 01期

关键词：

lipid rafts; Alzheimer's disease; AICD (APP intracellular domain); flotillin;

D O I：

10.1016/j.bbrc.2006.01.156

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Amyloid beta (A beta) is a pathological hallmark of Alzheimer's disease (AD). It is derived from the amyloid precursor protein (APP) by two sequential proteolytic cleavages, which also generate the APP intracellular domain (AICD). The precise cellular function(s) of AICD still remain obscure. To elucidate the roles of AICD in the development of AD, a yeast two-hybrid system was used to screen a human brain cDNA library for proteins interacting directly with AICD. One of the potential AICD-interacting proteins identified from our screening result is a lipid raft-associated protein, flotillin-1. The interaction was confirmed by glutathione S-transferase pull-down and coimmunoprecipitation studies. Since lipid raft has been suggested to play an important role in signal transduction as well as the pathogenic development of neurodegenerative diseases, it is proposed that flotillin-1 may recruit APP to lipid rafts and therefore participate in the localization and processing of APP. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：266 / 272

页数：7

共 42 条

[31] Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: some APP in large complexes [J].