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Molecular Dissection of the Interaction between Amyloid Precursor Protein and Its Neuronal Trafficking Receptor SorLA/LR11
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    Molecular Dissection of the Interaction between Amyloid Precursor Protein and Its Neuronal Trafficking Receptor SorLA/LR11
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    Max-Delbrueck-Center for Molecular Medicine, Berlin, 13125 Berlin, Germany, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts 02129, Department of Medical Biochemistry, University of Aarhus, 8000 Aarhus C, Denmark, Department of Pathology and Centre for Neurosciences, The University of Melbourne, Victoria 3010, Australia, The Mental Health Research Institute of Victoria, Parkville, Victoria 3052, Australia, and Biota Structural Biology Laboratory, St. Vincent's Institute of Medical Research, 41 Victoria Parade, Fitzroy, Victoria 3065, Australia
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    Biochemistry

    Cite this: Biochemistry 2006, 45, 8, 2618–2628
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    https://doi.org/10.1021/bi052120v
    Published February 4, 2006
    Copyright © 2006 American Chemical Society

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    SorLA/LR11 is a sorting receptor that regulates the intracellular transport and processing of the amyloid precursor protein (APP) in neurons. SorLA/LR11-mediated binding results in sequestration of APP in the Golgi and in protection from processing into the amyloid-β peptide (Aβ), the principal component of senile plaques in Alzheimer's disease (AD). To gain insight into the molecular mechanisms governing sorLA and APP interaction, we have dissected the respective protein interacting domains. Using a fluorescence resonance energy transfer (FRET) based assay of protein proximity, we identified binding sites in the extracellular regions of both proteins. Fine mapping by surface plasmon resonance analysis and analytical ultracentrifugation of recombinant APP and sorLA fragments further narrowed down the binding domains to the cluster of complement-type repeats in sorLA that forms a 1:1 stoichiometric complex with the carbohydrate-linked domain of APP. These data shed new light on the molecular determinants of neuronal APP trafficking and processing and on possible targets for intervention with senile plaque formation in patients with AD.

    Copyright © 2006 American Chemical Society

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     This work was funded in part by grants from the DFG and BMBF (to T.E.W.), the Lundbeck Foundation, the American Health Assistance Foundation, and the Danish Medical Research Council (to O.M.A.), the NIH (to B.T.H.), and The National Health and Medical Research Council of Australia (to C.L.M., M.W.P., W.J.M., and R.C.).

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     Address correspondence to this author. Tel:  +49-30-9406-3749. Fax:  +49-30-9406-3382. E-mail:  [email protected].

     Max-Delbrueck-Center for Molecular Medicine.

    §

     Massachusetts General Hospital, Harvard Medical School.

     University of Aarhus.

     Department of Pathology, The University of Melbourne.

    #

     The Mental Health Research Institute of Victoria.

     St. Vincent's Institute of Medical Research.

     Centre for Neurosciences, The University of Melbourne.

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    One figure showing control sensorgrams for the surface plasmon resonance analysis. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Biochemistry

    Cite this: Biochemistry 2006, 45, 8, 2618–2628
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    https://doi.org/10.1021/bi052120v
    Published February 4, 2006
    Copyright © 2006 American Chemical Society

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