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• W2912479666 abstract "Abstract The generation of the amyloid‐β (Aβ) peptides from the amyloid precursor protein ( APP ) through sequential proteolysis by β‐ and γ‐secretases is a key pathological event in the initiation and propagation of Alzheimer's disease. Aβ and the transcriptionally active APP intracellular domain are generated preferentially from the APP 695 isoform compared to the longer APP 751 isoform. As the Aβ and amyloid precursor protein intracellular domain produced from cleavage of APP 695 and APP 751 are identical we hypothesised that the two isoforms have differences within their interactomes which mediate the differential processing of the two isoforms. To investigate this, we applied a proteomics‐based approach to identify differences in the interactomes of the APP 695 and APP 751 isoforms. Using stable isotope labelling of amino acids in cell culture and quantitative proteomics, we compared the interactomes of APP 695 and APP 751 expressed in human SH ‐ SY 5Y cells. Through this approach, we identified enrichment of proteins involved in mitochondrial function, the nuclear pore and nuclear transport specifically in the APP 695 interactome. Further interrogation of the APP interactome and subsequent experimental validation (co‐immunoprecipitation and si RNA knockdown) revealed GAP 43 as a specific modulator of APP 751 proteolysis, altering Aβ generation. Our data indicate that interrogation of the APP interactome can be exploited to identify proteins which influence APP proteolysis and Aβ production in an isoform dependent‐manner. image Cover Image for this issue: doi: 10.1111/jnc.14504 ." @default.
• W2912479666 created "2019-02-21" @default.
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• W2912479666 date "2019-02-14" @default.
• W2912479666 modified "2023-10-01" @default.
• W2912479666 title "Quantitative interaction proteomics reveals differences in the interactomes of amyloid precursor protein isoforms" @default.
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• W2912479666 doi "https://doi.org/10.1111/jnc.14666" @default.
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