ArticleMolecular neurodegeneration2012
FE65 as a link between VLDLR and APP to regulate their trafficking and processing.
Article in Molecular neurodegeneration, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- VLDLR: A Multifunctional receptor in diverse pathophysiological processes.Cell communication and signaling : CCS · 2026Review
- The AICD interactome: implications in neurodevelopment and neurodegeneration.Biochemical Society transactions · 2024Review
- Suppression of the amyloidogenic metabolism of APP and the accumulation of Aβ by alcadein α in the brain during aging.Scientific reports · 2024Article
- Reelin Signaling in Neurodevelopmental Disorders and Neurodegenerative Diseases.Brain sciences · 2023Review
- ARNO is recruited by the neuronal adaptor FE65 to potentiate ARF6-mediated neurite outgrowth.Open biology · 2022Article
- Fe65: A Scaffolding Protein of Actin Regulators.Cells · 2021Review
- RIP at the Synapse and the Role of Intracellular Domains in Neurons.Neuromolecular medicine · 2020Review
- Candidate-based screening via gene modulation in human neurons and astrocytes implicates FERMT2 in Aβ and TAU proteostasis.Human molecular genetics · 2019Article
- Degradation routes of trafficking-defective VLDLR mutants associated with Dysequilibrium syndrome.Scientific reports · 2018Article
- APP Protein Family Signaling at the Synapse: Insights from Intracellular APP-Binding Proteins.Frontiers in molecular neuroscience · 2017Review
- Functional Roles of the Interaction of APP and Lipoprotein Receptors.Frontiers in molecular neuroscience · 2017Review
- FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.Scientific reports · 2016Article
- APP Receptor? To Be or Not To Be.Trends in pharmacological sciences · 2016Review
- Immununochemical Markers of the Amyloid Cascade in the Hippocampus in Motor Neuron Diseases.Frontiers in neurology · 2016Article
- Phosphorylation of FE65 Ser610 by serum- and glucocorticoid-induced kinase 1 modulates Alzheimer's disease amyloid precursor protein processing.The Biochemical journal · 2015Article
- FE65 and FE65L1 amyloid precursor protein-binding protein compound null mice display adult-onset cataract and muscle weakness.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- Very low density lipoprotein receptor regulates dendritic spine formation in a RasGRF1/CaMKII dependent manner.Biochimica et biophysica acta · 2015Article
- More than cholesterol transporters: lipoprotein receptors in CNS function and neurodegeneration.Neuron · 2014Review
- Amyloid beta a4 precursor protein-binding family B member 1 (FE65) interactomics revealed synaptic vesicle glycoprotein 2A (SV2A) and sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) as new binding proteins in the human brain.Molecular & cellular proteomics : MCP · 2014Article
- Fyn tyrosine kinase increases Apolipoprotein E Receptor 2 levels and phosphorylation.PloS one · 2014Article
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Authors and funding
12 authors at 6 institutions in 3 countries.
Funding
Abstract
backgroundSeveral studies found that FE65, a cytoplasmic adaptor protein, interacts with APP and LRP1, altering the trafficking and processing of APP. We have previously shown that FE65 interacts with the ApoE receptor, ApoER2, altering its trafficking and processing. Interestingly, it has been shown that FE65 can act as a linker between APP and LRP1 or ApoER2. In the present study, we tested whether FE65 can interact with another ApoE receptor, VLDLR, thereby altering its trafficking and processing, and whether FE65 can serve as a linker between APP and VLDLR.
resultsWe found that FE65 interacted with VLDLR using GST pull-down and co-immunoprecipitation assays in COS7 cells and in brain lysates. This interaction occurs via the PTB1 domain of FE65. Co-transfection with FE65 and full length VLDLR increased secreted VLDLR (sVLDLR); however, the levels of VLDLR C-terminal fragment (CTF) were undetectable as a result of proteasomal degradation. Additionally, FE65 increased cell surface levels of VLDLR. Moreover, we identified a novel complex between VLDLR and APP, which altered trafficking and processing of both proteins. Furthermore, immunoprecipitation results demonstrated that the presence of FE65 increased the interaction between APP and VLDLR in vitro and in vivo.
conclusionsThese data suggest that FE65 can regulate VLDLR trafficking and processing. Additionally, the interaction between VLDLR and APP altered both protein's trafficking and processing. Finally, our data suggest that FE65 serves as a link between VLDLR and APP. This novel interaction adds to a growing body of literature indicating trimeric complexes with various ApoE Receptors and APP.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.