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• W2912931473 abstract "SUMMARY Mitochondrial dysfunction and proteostasis failure frequently coexist as hallmarks of neurodegenerative disease. How these pathologies are related is not well understood. Here we describe a phenomenon termed MISTERMINATE ( mi tochondrial s tress-induced translational term ination impairment a n d protein c a rboxyl terminal e xtension), which mechanistically links mitochondrial dysfunction with proteostasis failure. We show that mitochondrial dysfunction impairs translational termination of nuclear-encoded mitochondrial mRNAs including complex-I 30kD subunit ( C-I30 ) mRNA, occurring on mitochondrial surface in Drosophila and mammalian cells. Ribosomes stalled at the normal stop codon continue to add to the C-terminus of C-I30 certain amino acids non-coded by mRNA template. C-terminally-extended C-I30 is toxic when assembled into C-I and forms aggregates in the cytosol. Enhancing co-translational quality control prevents C-I30 C-terminal extension and rescues mitochondrial and neuromuscular degeneration in a Parkinson’s disease model. These findings emphasize the importance of efficient translation termination and reveal unexpected link between mitochondrial health and proteome homeostasis mediated by MISTERMINATE." @default.
• W2912931473 created "2019-02-21" @default.
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• W2912931473 date "2019-02-19" @default.
• W2912931473 modified "2023-09-26" @default.
• W2912931473 title "MISTERMINATE Mechanistically Links Mitochondrial Dysfunction with Proteostasis Failure" @default.
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• W2912931473 doi "https://doi.org/10.1101/554634" @default.
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