Phosphorylation of FE65 Ser610 by serum- and glucocorticoid-induced kinase 1 modulates Alzheimer's disease amyloid precursor protein processing.
作者： Wan Ning Vanessa Chow , Jacky Chi Ki Ngo , Wen Li , Yu Wai Chen , Ka Ming Vincent Tam
DOI: 10.1042/BJ20141485
关键词:
摘要: Alzheimer9s disease (AD) is a fatal neurodegenerative affecting 36 million people worldwide. Genetic and biochemical research indicate that the excessive generation of amyloid-β peptide (Aβ) from amyloid precursor protein (APP), major part AD pathogenesis. FE65 brain-enriched adaptor binds to APP. However, role in APP processing mechanisms regulate binding are not fully understood. In present study, we show serum- glucocorticoid-induced kinase 1 (SGK1) phosphorylates on Ser 610 this phosphorylation attenuates We also promotes amyloidogenic inhibits effect. Furthermore, found effect linked FE65 in metabolic turnover via proteasome. Thus influences degradation proteasome by SGK1 regulates APP, processing.
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biochemj.org参考文章(65)
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