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- W3202053802 abstract "Abstract The contact sites between ER and mitochondria regulate several cellular processes including inter-organelle lipid transport, calcium homeostasis and autophagy. However, the mechanisms that regulate the dynamics and functions of these contact sites remain unresolved. We show that annulate lamellae (AL), a relatively unexplored subcellular structure representing subdomains of ER enriched with a subset of nucleoporins, are present at ER-mitochondria contact sites (ERMCS). Depletion of one of the AL-resident nucleoporins, Nup358, results in increased contacts between ER and mitochondria. Mechanistically, Nup358 modulates ERMCS dynamics by restricting mTORC2/Akt signalling. Our results suggest that growth factor-mediated remodelling of ERMCS depends on a reciprocal binding of Nup358 and mTOR to the ERMCS tethering complex consisting of VAPB and PTPIP51. Furthermore, Nup358 also interacts with IP3R, an ERMCS-enriched Ca 2+ channel, and controls Ca 2+ release from the ER. Consequently, depletion of Nup358 leads to elevated cytoplasmic Ca 2+ and autophagy via activation of Ca 2+ /CaMKK2/AMPK axis. Our study thus uncovers a novel role for AL, particularly for Nup358, in regulating mTORC2-mediated ERMCS remodelling and Ca 2+ -directed autophagy, possibly via independent mechanisms." @default.
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- W3202053802 date "2021-10-01" @default.
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- W3202053802 title "Nup358 regulates remodelling of ER-mitochondrial contact sites and autophagy" @default.
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- W3202053802 doi "https://doi.org/10.1101/2021.10.01.462723" @default.
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