Phosphorylation of LRP1 regulates the interaction with Fe65

12Citations
Citations of this article
32Readers
Mendeley users who have this article in their library.

Abstract

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.

Cite

CITATION STYLE

APA

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. https://doi.org/10.1016/j.febslet.2011.09.028

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free