Essential role of FE65 phosphorylation in APP metabolism
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Abstract

Aggregation of amyloid-β peptide (Aβ), derived from the aberrant processing of amyloid precursor protein (APP), is believed to be a crucial event in the pathogenesis of Alzheimer’s disease. FE65 is a neural enriched adaptor protein has been shown to interact with APP via its PTB1 domain. FE65/APP interaction is reported to stimulate APP processing. Therefore it is essential to understand the mechanism(s) by which FE65/APP interaction is regulated. FE65 is a phospho-protein with several reported phosphorylation sites. However, the biological significance of FE65 phosphorylation is largely unknown. In this study, we showed that serum- and glucocorticoid-induced kinase 1 (SGK1) phosphorylates FE65 on serine-610 (S610)and to attenuate FE65/APP interaction. Importantly, FE65 S610 phosphorylation suppresses the stimulatory effect of FE65 on APP processing. Moreover, the effect of FE65 S610 phosphorylation on APP processing is linked to a role of FE65 in metabolic turnover of APP via the proteasome. Together, our work suggests that FE65 phosphorylation can influence FE65- mediated APP processing

Acceptance Date13/11/2016
All Author(s) ListKF Lau, W Chow, W Li, HYE Chan, J Ngo
Name of ConferenceNeuroscience 2016
Start Date of Conference12/11/2016
End Date of Conference16/11/2016
Place of ConferenceSan Diego
Country/Region of ConferenceUnited States of America
Year2016
LanguagesEnglish-United States

Last updated on 2018-21-01 at 21:38