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

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AbstractAberrant 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.
Acceptance Date22/06/2017
All Author(s) ListLau Kwok Fai, Chau Dik Long, Li Wen, Ngo Jacky Chi Ki
Name of ConferenceNeuroscience 2017
Start Date of Conference11/11/2017
End Date of Conference15/11/2017
Place of ConferenceWashington DC
Country/Region of ConferenceUnited States of America
LanguagesEnglish-United States
KeywordsFE65, GULP1, Amyloid Precursor Protein

Last updated on 2018-14-05 at 15:35