Phosphorylation of LRP1 regulates the interaction with Fe65
Copyright policy )Phosphorylation of LRP1 regulates the interaction with Fe65
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.
- European Bioinformatics Institute United Kingdom
- European Molecular Biology Laboratory Germany
- Heidelberg University Germany
Amino Acid Motifs, Nuclear Proteins, Nerve Tissue Proteins, Protein Structure, Tertiary, Amyloid beta-Protein Precursor, Fe65, Alzheimer Disease, Multiprotein Complexes, Phosphotyrosine binding domain (PTB), LDL receptor-related protein 1 (LRP1), Humans, NPXY, Phosphorylation, Amyloid precursor protein (APP), Low Density Lipoprotein Receptor-Related Protein-1
Amino Acid Motifs, Nuclear Proteins, Nerve Tissue Proteins, Protein Structure, Tertiary, Amyloid beta-Protein Precursor, Fe65, Alzheimer Disease, Multiprotein Complexes, Phosphotyrosine binding domain (PTB), LDL receptor-related protein 1 (LRP1), Humans, NPXY, Phosphorylation, Amyloid precursor protein (APP), Low Density Lipoprotein Receptor-Related Protein-1
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