Structural aspects and physiological consequences of APP/APLP trans-dimerization
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Published on: January 24, 2025
Frederik Baumkötter1, Katja Wagner, Simone Eggert
1Department of Human Biology and Human Genetics, Technical University of Kaiserslautern, Erwin-Schrödinger-Straße 13, 67663 Kaiserslautern, Germany.
Abstract:
The amyloid precursor protein (APP) is one of the key proteins in Alzheimer's disease (AD), as it is the precursor of amyloid β (Aβ) peptides accumulating in amyloid plaques. The processing of APP and the pathogenic features of especially Aβ oligomers have been analyzed in detail. Remarkably, there is accumulating evidence from cell biological and structural studies suggesting that APP and its mammalian homologs, the amyloid precursor-like proteins (APLP1 and APLP2), participate under physiological conditions via trans-cellular dimerization in synaptogenesis. This offers the possibility that loss of synapses in AD might be partially explained by dysfunction of APP/APLPs cell adhesion properties. In this review, structural characteristics of APP trans-cellular interaction will be placed critically in context with its putative physiological functions focusing on cell adhesion and synaptogenesis.
