Phosphorylation of LRP1 regulates the interaction with Fe65

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Neuronal Fe65 is a central adapter for the intracellular protein network of Alzheimer's disease related amyloid precursor protein (APP). It contains a unique tandem array of phosphotyrosine-binding (PTB) domains that recognize NPXY internalization motifs present in the intracellular domains of APP (AICD) and the low-density lipoprotein receptor-related protein LRP1 (LICD). The ternary APP/Fe65/LRP1 complex is an important mediator of APP processing and affects β-amyloid peptide production. Here we dissect by biochemical and biophysical methods the direct interactions within the ternary complex and reveal a phosphorylation-dependent insulin receptor substrate (IRS-) like interaction of the distal NPVY 4507 motif of LICD with Fe65-PTB1. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.




Klug, W., Dietl, A., Simon, B., Sinning, I., & Wild, K. (2011). Phosphorylation of LRP1 regulates the interaction with Fe65. FEBS Letters, 585(20), 3229–3235.

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