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A more recent version of this article appeared on August 25, 2006
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M600728200v1
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Papers In Press, published online ahead of print April 25, 2006
J. Biol. Chem, 10.1074/jbc.M600728200
Submitted on January 24, 2006
Accepted on April 25, 2006

FE65 Interaction with the apoE receptor ApoEr2

Hyang-Sook Hoe, Laura Ann Magill, Suzanne Guenette, Zhanyan Fu, Stefano Vicini, and G. William Rebeck

Neuroscience, Georgetwon University, Washington, DC 20007

Corresponding Author: gwr2{at}georgetown.edu

The adaptor protein FE65 interacts with the ß-amyloid precursor protein (APP) via its C-terminal PTB domain, and affects APP processing and A production. Our previous data demonstrated that the apoE receptor ApoEr2 co-precipitated with APP, and suggested that there are extracellular and intracellular interactions between these two transmembrane proteins. We hypothesized that FE65 acts as an intracellular link between ApoEr2 and APP. Co-immunoprecipitation experiments in COS7 cells demonstrated an interaction between ApoEr2 and FE65 that depended on the N-terminal PTB domain of FE65. Full–length FE65 increased co-immunoprecipitation of ApoEr2 and APP. Full length FE65 also increased surface expression of ApoEr2, as determined by surface protein biotinylation and live cell surface staining. Constructs containing both the C- and N-terminal PTB domains of FE65 increased secreted APP, secreted ApoEr2, APP CTF, and ApoEr2 CTF, but constructs containing only single PTB domains did not affect APP or ApoEr2 processing. In addition, full-length FE65 decreased A to a significantly greater extent than individual FE65 domains. These data suggest that FE65 can bind APP and ApoEr2 at the same time and affect the processing of each.


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