Structural aspects and physiological consequences of APP/APLP trans-dimerization.

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.

journal_name

Exp Brain Res

authors

Baumkötter F,Wagner K,Eggert S,Wild K,Kins S

doi

10.1007/s00221-011-2878-6

subject

Has Abstract

pub_date

2012-04-01 00:00:00

pages

389-95

issue

3-4

eissn

0014-4819

issn

1432-1106

journal_volume

217

pub_type

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