Investigation of the mechanisms that APP interacting proteins regulate in APP processing
Refereed conference paper presented and published in conference proceedings

摘要Aberrant amyloid precursor protein (APP) processing to overproduce amyloid-beta peptide (Aβ) is believed to be a crucial event in Alzheimer's disease (AD) pathogenesis. Although several strategies have been proposed/tested to reduce Aβ production, severe side-effects and/or unsatisfied effectiveness have been reported for some approaches. Alternative strategies for treating the disease are therefore desirable. Increasing evidence indicates that APP-interacting proteins alter APP metabolism including FE65 and GULP1. Targeting APP/AIP interactions could be possible strategies to reduce Aβ production. However, the mechanisms by which the interactions are regulated remain elusive. Protein phosphorylation is a common mechanism to regulate protein-protein interaction. In fact, we identified kinases that phosphorylate FE65 and GULP1. The impacts of such phosphorylation of FE65 and GULP1 on APP processing were investigated. Our study shed valuable light on the regulatory mechanisms of FE65/APP and GULP1/APP interactions, and might provide essential information for the development of alternative therapeutic strategies for AD.
著者Lau Kwok Fai, Chau Dik Long, Li Wen, Ngo Jacky Chi Ki
會議名稱Neuroscience 2017
會議地點Washington DC
關鍵詞FE65, GULP1, Amyloid Precursor Protein

上次更新時間 2018-14-05 於 15:35