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A tRNA processing enzyme is a key regulator of the mitochondrial unfolded
Held JP, Feng G, Saunders BR, Pereira CV, Burkewitz K, Patel MR
Submitted Externally on 6/21/2022
Volume : Pages
The mitochondrial unfolded protein response (UPRmt) has emerged as a predominant
mechanism that preserves mitochondrial function. Consequently, multiple pathways
likely exist to modulate UPRmt. We discovered that the tRNA processing enzyme,
homolog of ELAC2 (HOE-1), is key to UPRmt regulation in Caenorhabditis elegans.
We find that nuclear HOE-1 is necessary and sufficient to robustly activate
UPRmt. We show that HOE-1 acts via transcription factors ATFS-1 and DVE-1 that
are crucial for UPRmt. Mechanistically, we show that HOE-1 likely mediates its
effects via tRNAs, as blocking tRNA export prevents HOE-1-induced UPRmt.
Interestingly, we find that HOE-1 does not act via the integrated stress
response, which can be activated by uncharged tRNAs, pointing toward its
reliance on a new mechanism. Finally, we show that the subcellular localization
of HOE-1 is responsive to mitochondrial stress and is subject to negative
regulation via ATFS-1. Together, we have discovered a novel RNA-based cellular
pathway that modulates UPRmt.
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Financial support for this work was provided by the NIDDK Mouse Metabolic Phenotyping Centers (National MMPC, RRID:SCR_008997,
) under the MICROMouse Program, grants DK076169.
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