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Kaden, D.* ; Munter, L.M.* ; Reif, B. ; Multhaup, G.*

The amyloid precursor protein and its homologues: Structural and functional aspects of native and pathogenic oligomerization.

Eur. J. Cell Biol. 91, 234-239 (2012)

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Open Access Green as soon as Postprint is submitted to ZB.

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Over the last 25 years, remarkable progress has been made not only in identifying key molecules of Alzheimer's disease but also in understanding their meaning in the pathogenic state. One hallmark of Alzheimer pathology is the amyloid plaque. A major component of the extracellular deposit is the amyloid-beta (A beta) peptide which is generated from its larger precursor molecule, i.e., the amyloid precursor protein (APP) by consecutive cleavages. Processing is exerted by two enzymes, i.e., the beta-secretase and the gamma-secretase. We and others have found that the self-association of the amyloid peptide and the dimerization and oligomerization of these proteins is a key factor under native and pathogenic conditions. In particular, the A beta homodimer represents a nidus for plaque formation and a well defined therapeutic target. Further, dimerization of the APP was reported to increase generation of toxic A beta whereas heterodimerization with its homologues amyloid precursor like proteins (APLP1 and APLP2) decreased A beta formation. This review mainly focuses on structural features of the homophilic and heterophilic interactions among APP family proteins. The proposed contact sites are described and the consequences of protein dimerization on their functions and in the pathogenesis of Alzheimer's disease are discussed.

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Publication type Article: Journal article

Document type Review

Corresponding Author

Keywords Amyloid Precursor Protein (app) ; Aplp1 ; Aplp2 ; Dimer ; Homodimerization ; Heterodimerization ; Structure ; Amyloid-beta Generation

ISSN (print) / ISBN 0171-9335

e-ISSN 1618-1298

Journal European Journal of Cell Biology

Quellenangaben Volume: 91, Issue: 4, Pages: 234-239

Publisher Elsevier

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Structural Biology (STB)