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Cell interactions are promoted by transdimerization of APP family members, arranged as homo- or heterocomplexes in synaptic membranes

Soba, Peter and Eggert, Simone and Wagner, Katja and Zentgraf, Hanswalter and Siehl, Katjuscha and Kreger, Sylvia and Loewer, Alexander and Langer, Andreas and Merdes, Gunter and Paro, Renato and Masters, Colin L. and Müller, Ulrike and Kins, Stefan and Beyreuther, Konrad (2006):
Cell interactions are promoted by transdimerization of APP family members, arranged as homo- or heterocomplexes in synaptic membranes.
In: The EMBO journal, 25 (3), p. 653. ISSN 0261-4189,
[Article]

Abstract

The amyloid precursor protein (APP) plays a central role in Alzheimer's disease, but its physiological function and that of its mammalian paralogs, the amyloid precursor-like proteins 1 and 2 (APLPs), is still poorly understood. APP has been proposed to form dimers, a process that could promote cell adhesion via trans-dimerization. We investigated the dimerization and cell adhesion properties of APP/APLPs and provide evidence that all three paralogs are capable of forming homo- and heterocomplexes. Moreover, we show that trans-interaction of APP family proteins promotes cell-cell adhesion in a homo- and heterotypic fashion and that endogenous APLP2 is required for cell-cell adhesion in mouse embryonic fibroblasts. We further demonstrate interaction of all the three APP family members in mouse brain, genetic interdependence, and molecular interaction of APP and APLPs in synaptically enriched membrane compartments. Together, our results provide evidence that homo- and heterocomplexes of APP/APLPs promote trans-cellular adhesion in vivo.

Item Type: Article
Erschienen: 2006
Creators: Soba, Peter and Eggert, Simone and Wagner, Katja and Zentgraf, Hanswalter and Siehl, Katjuscha and Kreger, Sylvia and Loewer, Alexander and Langer, Andreas and Merdes, Gunter and Paro, Renato and Masters, Colin L. and Müller, Ulrike and Kins, Stefan and Beyreuther, Konrad
Title: Cell interactions are promoted by transdimerization of APP family members, arranged as homo- or heterocomplexes in synaptic membranes
Language: English
Abstract:

The amyloid precursor protein (APP) plays a central role in Alzheimer's disease, but its physiological function and that of its mammalian paralogs, the amyloid precursor-like proteins 1 and 2 (APLPs), is still poorly understood. APP has been proposed to form dimers, a process that could promote cell adhesion via trans-dimerization. We investigated the dimerization and cell adhesion properties of APP/APLPs and provide evidence that all three paralogs are capable of forming homo- and heterocomplexes. Moreover, we show that trans-interaction of APP family proteins promotes cell-cell adhesion in a homo- and heterotypic fashion and that endogenous APLP2 is required for cell-cell adhesion in mouse embryonic fibroblasts. We further demonstrate interaction of all the three APP family members in mouse brain, genetic interdependence, and molecular interaction of APP and APLPs in synaptically enriched membrane compartments. Together, our results provide evidence that homo- and heterocomplexes of APP/APLPs promote trans-cellular adhesion in vivo.

Journal or Publication Title: The EMBO journal
Journal volume: 25
Number: 3
Divisions: 10 Department of Biology
10 Department of Biology > Systems Biology of the Stress Response
Date Deposited: 02 Sep 2015 09:10
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