Protein-protein interactions in the assembly and subcellular trafficking of the BACE (beta-site amyloid precursor protein-cleaving enzyme) complex of Alzheimer's disease.
The correct assembly of the BACE (beta-site amyloid precursor protein-cleaving enzyme or beta-secretase) complex and its subsequent trafficking to cellular compartments where it associates with the APP (amyloid precursor protein) is essential for the production of Abeta (amyloid beta-peptide), the protein whose aggregation into senile plaques is thought to be responsible for the pathogenesis of AD (Alzheimer's disease). These processes rely upon both transient and permanent BACE-protein interactions. This review will discuss what is currently known about these BACE-protein interactions and how they may reveal novel therapeutic targets for the treatment of AD.
Parsons
R B
RB
Department of Basic Medical Sciences, St. George's, University of London, Cranmer Terrace, London SW17 0RE, U.K. r.parsons@sgul.ac.uk
Austen
B M
BM
D000544:Alzheimer Disease / Q000378:metabolism*; D053829:Amyloid Precursor Protein Secretases / Q000378:metabolism*; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D002784:Cholesterol / Q000378:metabolism; D019281:Dimerization; D006801:Humans; D019308:Palmitic Acid / Q000378:metabolism; D011485:Protein Binding; D021381:Protein Transport; D013347:Subcellular Fractions / Q000378:metabolism*
D019308:Palmitic Acid; D002784:Cholesterol; D053829:Amyloid Precursor Protein Secretases; D016282:Aspartic Acid Endopeptidases; C509280:BACE1 protein, human