Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2204935 | Trends in Cell Biology | 2008 | 4 Pages |
Abstract
Disruption of protein homeostasis in mitochondria elicits a cellular response, which upregulates mitochondrial chaperones and other factors that serve to remodel the mitochondrial-folding environment. In a recent study, Haynes and colleagues uncovered a novel signal transduction pathway underlying this process. The upstream mitochondrial component of this pathway is an orthologue of Escherichia coli ClpP, which functions in the bacterial heat-shock response. These findings suggest that molecular aspects of stress sensing might be conserved between bacteria and mitochondria.
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Authors
Sarah A. Broadley, F. Ulrich Hartl,