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Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

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FE65 as a link between VLDLR and APP to regulate their trafficking and processing.

Sonya B Dumanis¹, Kelly A Chamberlain, Yoo Jin Sohn

¹Department of Neuroscience, Georgetown University Medical Center, 3970 Reservoir Road NW, Washington, DC 20057-1464, USA.

Molecular Neurodegeneration

|March 21, 2012

Summary

FE65 adaptor protein links VLDLR and APP, altering their trafficking and processing. This interaction influences Alzheimer's disease pathways by affecting amyloid precursor protein (APP) and very-low-density lipoprotein receptor (VLDLR) interactions.

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Area of Science:

Neuroscience
Molecular Biology
Cell Biology

Background:

FE65 adaptor protein interacts with APP and LRP1, influencing APP processing.
FE65 also interacts with ApoE receptor ApoER2, affecting its trafficking.
FE65 acts as a linker between APP and LRP1 or ApoER2.

Purpose of the Study:

Investigate FE65 interaction with another ApoE receptor, VLDLR.
Determine if FE65 alters VLDLR trafficking and processing.
Ascertain if FE65 links APP and VLDLR.

Main Methods:

GST pull-down and co-immunoprecipitation assays in COS7 cells and brain lysates.
Analysis of VLDLR and APP processing fragments.
Assessment of cell surface protein levels.
In vitro and in vivo immunoprecipitation.

Main Results:

FE65 directly interacts with VLDLR via its PTB1 domain.
FE65 increases secreted VLDLR (sVLDLR) and cell surface VLDLR levels.
FE65 promotes the formation of a novel VLDLR-APP complex, altering both proteins' trafficking and processing.
FE65 enhances the interaction between APP and VLDLR.

Conclusions:

FE65 regulates VLDLR trafficking and processing.
The VLDLR-APP interaction, mediated by FE65, impacts protein processing.
FE65 acts as a linker between VLDLR and APP, forming trimeric complexes relevant to neurodegenerative disease research.