α-secretase ADAM IO physically interacts with β-secretase BACE1 in neurons and regulates CHL1 proteolysis
α-secretase ADAM IO physically interacts with β-secretase BACE1 in neurons and regulates CHL1 proteolysis作者机构：State Key Laboratory of Cell Biology CAS Center for Excellence in Molecular Cell Science Shanghai Institute of Biochemistry and Cell Biology Chinese Academy of Sciences University of Chinese Academy of Sciences Shanghai 200031 China Shanghai Key Laboratory of Signaling and Disease Research Collaborative Innovation Center for Brain Science School of Life Sciences and Technology Tongji University Shanghai 200092 China
出 版 物：《Journal of Molecular Cell Biology》 (分子细胞生物学报（英文版）)
年 卷 期：2018年第10卷第5期
页 面：411-422页
核心收录：
学科分类：0710[理学-生物学] 07[理学] 080202[工学-机械电子工程] 08[工学] 071006[理学-神经生物学] 0802[工学-机械工程]
基 金：supported by the Ministry of Science and Technology International Science & Technology Cooperation Program of China
主 题：secretase Alzheimer's disease ADAM10 BACE1 interact APP CHL1
摘 要：α-secretase and β-secretase are known to compete for amyloid precursor protein （APP） processing and thus play a vital role in Alzheimer＇s disease pathogenesis. A disintegrin and metaUoproteinase 10 （ADAM10） and β-site APP cleaving enzyme 1 （BACE1） mediate the major activities of α-secretase and β-secretase in brain and share various common substrates. However, whether they function separately or together is poorly understood. Here, we show that ADAM10 and BACE1 co-localize in the neurites of mouse primary neurons. Co-immunoprecipitation and fluorescence resonance energy transfer analysis revealed that ADAM10 and BACE1 interact with each other under both endogenous and exogenous conditions. In addition, we found that ADAMIO enhances the proteolysis of neural cell adhesion molecule close homolog of L1 （CHL1） by BACE1. Further studies found that ADAM10-BACE1 interaction interfering peptide LT52 attenuates the regulation of ADAM10 on BACEl-mediated cleavage of CHL1. Our data indicate that ADAM10-BACE1 interaction regulates the proteolysis of some specific substrates and may play a potential role in brain function.
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