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- W3133890450 abstract "SorLA/LR11 is a sorting receptor that regulates the intracellular transport and processing of the amyloid precursor protein (APP) in neurons. SorLA/LR11–mediated binding results in sequestration of APP in the Golgi and in protection from processing into the amyloid β–peptide (Aβ), the principal component of senile plaques in Alzheimer's disease (AD). To gain insights into the molecular mechanisms governing sorLA/LR11 and APP interaction, we dissect the respective protein interacting domains. Using a fluorescence resonance energy transfer (FRET)–based assay of protein proximity we identified binding sites in the extracellular regions of both proteins. Surface plasmon resonance analysis and analytical ultracentrifugation of recombinant APP and sorLA/LR11 fragments further narrowed down the binding domains. We showed that the cluster of complement–type repeats in sorLA/LR11 forms a 1:1 stoichiometric complex with part of the carbohydrate–linked domain of APP, and that this interaction is sufficient to promote association of both proteins in neurons. These data shed new light on the molecular determinants of neuronal APP trafficking and processing." @default.
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- W3133890450 date "2006-07-01" @default.
- W3133890450 modified "2023-09-27" @default.
- W3133890450 title "P3-423: Molecular dissection of the interaction between APP and its neuronal trafficking receptor SorLA/LR11" @default.
- W3133890450 doi "https://doi.org/10.1016/j.jalz.2006.05.1694" @default.
- W3133890450 hasPublicationYear "2006" @default.
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