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Dev Cell. 2007 Oct;13(4):467-80.

ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans.

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1
Kimmel Center for Biology and Medicine of Skirball Institute and Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA.

Abstract

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 (UPR(mt)) 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-like protein UBL-5, both of which are encoded by genes required for signaling the UPR(mt). Activation of the UPR(mt) 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 UPR(mt) 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 UPR(mt).

PMID:
17925224
DOI:
10.1016/j.devcel.2007.07.016
[Indexed for MEDLINE]
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