Homo- and heterodimerization of APP family members promotes intercellular adhesion.
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ABSTRACT:
SUBMITTER: Soba P
PROVIDER: S-EPMC1276707 | biostudies-literature | 2005 Oct
REPOSITORIES: biostudies-literature
Publications
Homo- and heterodimerization of APP family members promotes intercellular adhesion.
Soba Peter P Eggert Simone S Wagner Katja K Zentgraf Hanswalter H Siehl Katjuscha K Kreger Sylvia S Löwer Alexander A Langer Andreas A Merdes Gunter G Paro Renato R Masters Colin L CL Müller Ulrike U Kins Stefan S Beyreuther Konrad K
The EMBO journal 20050929 20
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 heterocomplex ...[more]
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