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Phosphorylation of LRP1 regulates the interaction with Fe65

Neuronal Fe65 is a central adapter for the intracellular protein network of Alzheimer’s diseaserelated amyloid precursor protein (APP). It contains a unique tandem array of phosphotyrosine-binding (PTB) domains that recognize NPXY internalization motifs present in the intracellulardomains of APP (AI...

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Main Authors: Klug, Wilfried (Author) , Dietl, Andreas (Author) , Simon, Bernd (Author) , Sinning, Irmgard (Author) , Wild, Klemens (Author)
Format: Article (Journal)
Language:English
Published: 29 September 2011
In: FEBS letters
Year: 2011, Volume: 585, Issue: 20, Pages: 3229-3235
ISSN:1873-3468
DOI:10.1016/j.febslet.2011.09.028
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.febslet.2011.09.028
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2011.09.028
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Author Notes:Wilfried Klug, Andreas Dietl, Bernd Simon, Irmgard Sinning, Klemens Wild

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520 |a Neuronal Fe65 is a central adapter for the intracellular protein network of Alzheimer’s diseaserelated amyloid precursor protein (APP). It contains a unique tandem array of phosphotyrosine-binding (PTB) domains that recognize NPXY internalization motifs present in the intracellulardomains of APP (AICD) and the low-density lipoprotein receptor-related protein LRP1 (LICD). Theternary APP/Fe65/LRP1 complex is an important mediator of APP processing and affectsb-amyloidpeptide production. Here we dissect by biochemical and biophysical methods the direct interactionswithin the ternary complex and reveal a phosphorylation-dependent insulin receptor substrate(IRS-) like interaction of the distal NPVY4507motif of LICD with Fe65-PTB1. 
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