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BACE1 interacts with lipid raft proteins
Author(s) -
Hattori Chinatsu,
Asai Masashi,
Onishi Hayato,
Sasagawa Noboru,
Hashimoto Yasuhiro,
Saido Takaomi C.,
Maruyama Kei,
Mizutani Shigehiko,
Ishiura Shoichi
Publication year - 2006
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20981
Subject(s) - lipid raft , amyloid precursor protein secretase , amyloid precursor protein , presenilin , alpha secretase , microbiology and biotechnology , raft , chemistry , p3 peptide , amyloid (mycology) , alzheimer's disease , biochemistry , biology , cholesterol , disease , medicine , inorganic chemistry , organic chemistry , copolymer , polymer
A neuropathological hallmark of Alzheimer's disease is the presence of amyloid plaques in the brain. Amyloid‐β peptide (Aβ) is the major constituent of the plaques and is generated by proteolytic cleavages of amyloid precursor protein (APP) by β‐ and γ‐secretases. Growing evidence shows that lipid rafts are critically involved in regulating the Aβ generation. In support of this, APP, Aβ, and presenilins have been found in lipid rafts. Although cholesterol plays a crucial role in maintaining lipid rafts, functions of other components in the generation of Aβ are unknown. Caveolins (CAVs) and flotillins (FLOTs) are principal proteins related to lipid rafts and have been suggested to be involved in APP processing. Here, we report that FLOT‐1 binds to BACE1 (beta‐site APP cleaving enzyme 1) and that overexpression of CAV‐1 or FLOT‐1 results in recruiting BACE1 into lipid rafts and influence on β‐secretase activity in cultured cells. Our results show that both CAV‐1 and FLOT‐1 may modulate β‐secretase activity by interacting with BACE1. © 2006 Wiley‐Liss, Inc.