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- W2907800642 abstract "The mechanisms of mitochondrial dysfunction in Alzheimer’s Disease (AD) are incompletely understood. Using two-photon fluorescence lifetime microscopy of NAD(P)H and tracking brain oxygen metabolism with multi-parametric photoacoustic microscopy, we show that activation of lysosomal mechanistic target of rapamycin complex 1 (mTORC1) by insulin or amino acids stimulates mitochondrial activity and regulates mitochondrial DNA synthesis in neurons. Amyloid-β oligomers, which are precursors of amyloid plaques in AD brain and stimulate mTORC1 protein kinase activity at the plasma membrane, but not at lysosomes, block this nutrient-induced mitochondrial activity (NiMA) by a mechanism dependent on tau, which forms neurofibrillary tangles in AD brain. NiMA was also disrupted in fibroblasts derived from a patient with tuberous sclerosis complex, a genetic disorder that causes dysregulation of lysosomal mTORC1. Thus, lysosomal mTORC1 couples nutrient availability to mitochondrial activity, and links mitochondrial dysfunction to AD by a mechanism dependent on soluble building blocks of plaques and tangles." @default.
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- W2907800642 date "2018-01-01" @default.
- W2907800642 modified "2023-09-23" @default.
- W2907800642 title "Nutrient-induced Mitochondrial Activation (NiMA): A Novel Lysosome-to-Mitochondria Signaling Pathway Disrupted by Amyloid-- Oligomers" @default.
- W2907800642 doi "https://doi.org/10.2139/ssrn.3188445" @default.
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