Yeast Two-Hybrid Screening for Proteins that Interact with the Extracellular Domain of Amyloid Precursor Protein  

作　　者：You Yu Yinan Li Yan Zhang 

机构地区：[1]State Key Laboratory of Membrane Biology, College of Life Sciences, PKU-IDG/Mc Govern Institute for Brain Research,Peking University

出　　处：《Neuroscience Bulletin》2016年第2期171-176,共6页神经科学通报（英文版）

基　　金：supported by the National Natural Science Foundation of China for Distinguished Young Scholars(81425009);the Beijing Natural Science Foundation,China(7142085);the Peking University Collaborative Fund,China(464-10606-00416)

摘　　要：Alzheimer＇s disease（AD） is a neurodegenerative disorder in which amyloid b plaques are a pathological characteristic. Little is known about the physiological functions of amyloid b 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.Alzheimer＇s disease（AD） is a neurodegenerative disorder in which amyloid b plaques are a pathological characteristic. Little is known about the physiological functions of amyloid b 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.

关 键 词：Amyloid precursor protein Alzheimer’s disease Yeast two-hybrid screening Cell death Pelizaeus-Merzbacher disease 

分 类 号：R749.16[医药卫生—神经病学与精神病学]