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• W1886846543 abstract "Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events. However, the role of O-GlcNAcylation in neurodegenerative diseases such as Alzheimer's disease (AD) is poorly understood. Mitochondrial adenosine 5′-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi. Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells. Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity. Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity. These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A." @default.
• W1886846543 created "2016-06-24" @default.
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• W1886846543 date "2015-09-10" @default.
• W1886846543 modified "2023-10-12" @default.
• W1886846543 title "Mitochondrial ATP synthase activity is impaired by suppressed<i>O</i>-GlcNAcylation in Alzheimer's disease" @default.
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• W1886846543 doi "https://doi.org/10.1093/hmg/ddv358" @default.
• W1886846543 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5007609" @default.
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• W1886846543 hasPublicationYear "2015" @default.
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