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• W2488511372 startingPage "e0159989" @default.
• W2488511372 abstract "The mitochondrial unfolded protein response (UPRmt) is a surveillance pathway that defends proteostasis in the “powerhouse” of the cell. Activation of the UPRmt protects against stresses imposed by reactive oxygen species, respiratory chain deficits, and pathologic bacteria. Consistent with the UPRmt’s role in adaption, we found that either its pharmacological or genetic activation by ethidium bromide (EtBr) or RNAi of the mitochondrial AAA-protease spg-7 was sufficient to reduce death in an anoxia-based Caenorhabditis elegans model of ischemia-reperfusion injury. The UPRmt-specific transcription factor atfs-1 was necessary for protection and atfs-1 gain-of-function (gf) mutants were endogenously protected from both death and dysfunction. Neurons exhibited less axonal degeneration following non-lethal anoxia-reperfusion (A-R) when the UPRmt was pre-activated, and consistent with the concept of mitochondrial stress leading to cell non-autonomous (ie. “remote”) effects, we found that restricted activation of the UPRmt in neurons decreased A-R death. However, expression of the atfs-1(gf) mutant in neurons, which resulted in a robust activation of a neuronal UPRmt, did not upregulate the UPRmt in distal tissues, nor did it protect the worms from A-R toxicity. These findings suggest that remote signaling requires additional component(s) acting downstream of de facto mitochondrial stress." @default.
• W2488511372 created "2016-08-23" @default.
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• W2488511372 date "2016-07-26" @default.
• W2488511372 modified "2023-10-04" @default.
• W2488511372 title "The Mitochondrial Unfolded Protein Response Protects against Anoxia in Caenorhabditis elegans" @default.
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• W2488511372 doi "https://doi.org/10.1371/journal.pone.0159989" @default.
• W2488511372 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4961406" @default.
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