Yeast Two-Hybrid Screening for Proteins that Interact with the Extracellular Domain of Amyloid Precursor Protein.
Alzheimer's disease (AD) is a neurodegenerative disorder in which amyloid β plaques are a pathological characteristic. Little is known about the physiological functions of amyloid β precursor protein (APP). Based on its structure as a type I transmembrane protein, it has been proposed that APP might be a receptor, but ... so far, no ligand has been reported. In the present study, 9 proteins binding to the extracellular domain of APP were identified using a yeast two-hybrid system. After confirming the interactions in the mammalian system, mutated PLP1, members of the FLRT protein family, and KCTD16 were shown to interact with APP. These proteins have been reported to be involved in Pelizaeus-Merzbacher disease (PMD) and axon guidance. Therefore, our results shed light on the mechanisms of physiological function of APP in AD, PMD, and axon guidance.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Animals, Gene Library, HEK293 Cells, Humans, Immunoprecipitation, Luminescent Proteins, Membrane Proteins, Mutation, Myelin Proteolipid Protein, Transfection, Two-Hybrid System Techniques
Adaptor Proteins, Signal Transducing, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Animals, Gene Library, HEK293 Cells, Humans, Immunoprecipitation, Luminescent Proteins, Membrane Proteins, Mutation, Myelin Proteolipid Protein, Transfection, Two-Hybrid System Techniques
Neurosci Bull
Date: Apr. 01, 2016
PubMed ID: 26960425
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