Mitochondrial stress signaling: a pathway unfolds

Trends in Cell Biology

Volumn 18, Issue 1, 2008, Pages 1-4

  Broadley, Sarah A ^a   Hartl, F Ulrich ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; ENDOPEPTIDASE CLP; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; PROTEIN UBL 5; TRANSCRIPTION FACTOR DVE 1; UNCLASSIFIED DRUG;

CELL STRESS; ESCHERICHIA COLI; HEAT SHOCK; HOMEOSTASIS; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN LOCALIZATION; RNA INTERFERENCE; SHORT SURVEY; SIGNAL TRANSDUCTION; UPREGULATION;

ANIMALS; BACTERIAL PHYSIOLOGY; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; ENDOPEPTIDASE CLP; GENE EXPRESSION REGULATION; HEAT-SHOCK PROTEINS; MITOCHONDRIA; MOLECULAR CHAPERONES; PROTEIN FOLDING; SIGNAL TRANSDUCTION; UBIQUITINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 37849022851     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2007.11.003     Document Type: Short Survey

References (25)

1. Hartl F.U., and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002) 1852-1858
2. Bukau B., et al. Molecular chaperones and protein quality control. Cell 125 (2006) 443-451
3. Kaushik S., et al. Chaperone-mediated autophagy and aging: a novel regulatory role of lipids revealed. Autophagy 3 (2007) 387-389
4. Esser C., et al. Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochim. Biophys. Acta 1695 (2004) 171-188
5. Benedetti C., et al. Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response. Genetics 174 (2006) 229-239
6. Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
7. Lindquist S. The heat-shock response. Annu. Rev. Biochem. 55 (1986) 1151-1191
8. Cotto J.J., and Morimoto R.I. Stress-induced activation of the heat-shock response: cell and molecular biology of heat-shock factors. Biochem. Soc. Symp. 64 (1999) 105-118
9. Murray J.I., et al. Diverse and specific gene expression responses to stresses in cultured human cells. Mol. Biol. Cell 15 (2004) 2361-2374
10. Martinus R.D., et al. Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome. Eur. J. Biochem. 240 (1996) 98-103
11. Zhao Q., et al. A mitochondrial specific stress response in mammalian cells. EMBO J. 21 (2002) 4411-4419
12. Yoneda T., et al. Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones. J. Cell Sci. 117 (2004) 4055-4066
13. Ryan M.T., and Hoogenraad N.J. Mitochondrial-nuclear communications. Annu. Rev. Biochem. 76 (2007) 701-722
14. Haynes C.M., et al. ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev. Cell 13 (2007) 467-480
15. Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66 (1997) 863-917
16. Fox T.D. Genetics of mitochondrial translation. In: Matthews M., et al. (Ed). Translational Regulation (1996), Cold Spring Harbor Laboratory Press 733-758
17. Nakagoshi H., et al. A novel homeobox gene mediates the Dpp signal to establish functional specificity within target cells. Genes Dev. 12 (1998) 2724-2734
18. Nakagomi K., et al. A novel DNA-binding motif in the nuclear matrix attachment DNA-binding protein SATB1. Mol. Cell. Biol. 14 (1994) 1852-1860
19. Dobreva G., et al. SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression. Genes Dev. 17 (2003) 3048-3061
20. Sauer R.T., et al. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119 (2004) 9-18
21. Flynn J.M., et al. Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes Dev. 18 (2004) 2292-2301
22. Kruger E., et al. Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor. EMBO J 20 (2001) 852-863
23. Young L., et al. Role of the ABC transporter Mdl1 in peptide export from mitochondria. Science 291 (2001) 2135-2138
24. Aldridge J.E., et al. Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements. PLoS ONE 2 (2007) e874
25. Horibe T., and Hoogenraad N.J. The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. PLoS ONE 2 (2007) e835