Characterization of presenilin-amyloid precursor interaction using bacterial expression and two-hybrid systems for human membrane proteins

Harnasch, Mona, Grau, Sandra, Behrends, Christian, Dove, Simon L., Hochschild, Ann, Iskandar, Maria-karnina, Xia, Weiming and Ehrmann, Michael ORCID: https://orcid.org/0000-0002-1927-260X 2004. Characterization of presenilin-amyloid precursor interaction using bacterial expression and two-hybrid systems for human membrane proteins. Molecular Membrane Biology 21 (6) , pp. 373-383. 10.1080/09687860400008429

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Abstract

An Escherichia coli system was used to produce the human membrane proteins presenilin 1 and amyloid precursor protein and to analyse their interaction. Our data indicate that the main binding site for amyloid precursor protein is located in the N-terminal three-transmembrane segments of presenilin and not in the proposed active site containing the two conserved aspartate residues. The data also suggest the presence of an additional segment of sufficient hydrophobicity at the C-terminus of PS1 to act potentially as a transmembrane segment. The implications of these findings for the function of γ-secretase are discussed.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	Informa Healthcare
ISSN:	0968-7688
Last Modified:	27 Oct 2022 08:46
URI:	https://orca.cardiff.ac.uk/id/eprint/63336

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