Journal
DEVELOPMENTAL CELL
Volume 13, Issue 4, Pages 467-480Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2007.07.016
Keywords
-
Categories
Funding
- NIDDK NIH HHS [DK47119] Funding Source: Medline
- NIEHS NIH HHS [ES08681] Funding Source: Medline
- NINDS NIH HHS [F32-NS050901] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available