期刊
DEVELOPMENTAL CELL
卷 13, 期 4, 页码 467-480出版社
CELL PRESS
DOI: 10.1016/j.devcel.2007.07.016
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资金
- NIDDK NIH HHS [DK47119] Funding Source: Medline
- NIEHS NIH HHS [ES08681] Funding Source: Medline
- NINDS NIH HHS [F32-NS050901] Funding Source: Medline
The cellular response to unfolded and misfolded proteins in the mitochondrial matrix is poorly understood. Here, we report on a genome-wide RNAi-based screen for genes that signal the mitochondrial unfolded protein response (UPRmt) in C. elegans. Unfolded protein stress in the mitochondria correlates with complex formation between a homeodomain-containing transcription factor DVE-1 and the small ubiquitin-fike protein UBL-5, both of which are encoded by genes required for signaling the UPRmt. Activation of the UPRmt correlates temporally and spatially with nuclear redistribution of DVE-1 and with its enhanced binding to the promoters of mitochondrial chaperone genes. These events and the downstream UPRmt are attenuated in animals with reduced activity of clpp-1, which encodes a mitochondrial matrix protease homologous to bacterial ClpP. As ClpP is known to function in the bacterial heat-shock response, our findings suggest that eukaryotes utilize component(s) from the protomitochondrial symbiont to signal the UPRmt.
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