Mitochondrial stress signaling: a pathway unfolds.
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.
Broadley
Sarah A
SA
Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
Hartl
F Ulrich
FU
D000818:Animals; D018407:Bacterial Physiological Phenomena; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism; D049071:Endopeptidase Clp / Q000235:genetics / Q000378:metabolism; D005786:Gene Expression Regulation; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D008928:Mitochondria / Q000502:physiology*; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D015398:Signal Transduction; D014452:Ubiquitins / Q000235:genetics / Q000378:metabolism
D029742:Caenorhabditis elegans Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D014452:Ubiquitins; C515527:Ubl-5 protein, C elegans; D049071:Endopeptidase Clp