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Visualization of Alzheimer's Disease Related ?-/?-/?-Secretase Ternary Complex by Bimolecular Fluorescence Complementation Based Fluorescence Resonance Energy Transfer.

ABSTRACT: The competitive ectodomain shedding of amyloid-? precursor protein (APP) by ?-secretase and ?-secretase, and the subsequent regulated intramembrane proteolysis by ?-secretase are the key processes in amyloid-? peptides (A?) generation. Previous studies indicate that secretases form binary complex and the interactions between secretases take part in substrates processing. However, whether ?-, ?- and ?-secretase could form ternary complex remains to be explored. Here, we adopted bimolecular fluorescence complementation in combination with fluorescence resonance energy transfer (BiFC-FRET) to visualize the formation of triple secretase complex. We show that the interaction between ?-secretase ADAM10 and ?-secretase BACE1 could be monitored by BiFC assay and the binding of APP to ?-/?-secretase binary complex was revealed by BiFC-FRET. Further, we observed that ?-secretase interacts with ?-/?-secretase binary complex, providing evidence that ?-, ?- and ?-secretase might form a ternary complex. Thus our study extends the interplay among Alzheimer's disease (AD) related ?-/?-/?-secretase.

SUBMITTER: Wang X 

PROVIDER: S-EPMC6277482 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Visualization of Alzheimer's Disease Related α-/β-/γ-Secretase Ternary Complex by Bimolecular Fluorescence Complementation Based Fluorescence Resonance Energy Transfer.

Wang Xin X   Pei Gang G  

Frontiers in molecular neuroscience 20181127

The competitive ectodomain shedding of amyloid-β precursor protein (APP) by α-secretase and β-secretase, and the subsequent regulated intramembrane proteolysis by γ-secretase are the key processes in amyloid-β peptides (Aβ) generation. Previous studies indicate that secretases form binary complex and the interactions between secretases take part in substrates processing. However, whether α-, β- and γ-secretase could form ternary complex remains to be explored. Here, we adopted bimolecular fluore  ...[more]

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