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

Mona Harnasch, Sandra Grau, Christian Behrends, Sinnon L. Dove, Ann Hochschild, Maria Karnina Iskandar, Weiming Xia, Michael Ehrmann

Research output: Contribution to journalArticle

6 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)373-383
Number of pages11
JournalMolecular Membrane Biology
Volume21
Issue number6
DOIs
StatePublished - Nov 2004

Keywords

  • Amyloid precursor protein
  • Human membrane proteins
  • Presenilin
  • Recombinant expression
  • Two-hybrid system

ASJC Scopus subject areas

  • Cell Biology

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