A role for mitochondria in NLRP3 inflammasome activation

Schroder, K. & Tschopp, J. The inflammasomes. Cell 140, 821–832 (2010)

Latz, E. The inflammasomes: mechanisms of activation and function. Curr. Opin. Immunol. 22, 28–33 (2010)

Kastner, D. L., Aksentijevich, I. & Goldbach-Mansky, R. Autoinflammatory disease reloaded: a clinical perspective. Cell 140, 784–790 (2010)

Franchi, L., Munoz-Planillo, R., Reimer, T., Eigenbrod, T. & Nunez, G. Inflammasomes as microbial sensors. Eur. J. Immunol. 40, 611–615 (2010)

Dostert, C. et al. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 320, 674–677 (2008)

Latz, E. NOX-free inflammasome activation. Blood 116, 1393–1394 (2010)

Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W. & Sheu, S.-S. Calcium, ATP, and ROS: a mitochondrial love-hate triangle. Am. J. Physiol. Cell Physiol. 287, C817–C833 (2004)

Li, N. et al. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 278, 8516–8525 (2003)

Goldman, S. J., Taylor, R., Zhang, Y. & Jin, S. Autophagy and the degradation of mitochondria. Mitochondrion 10, 309–315 (2010)

Levine, B. & Kroemer, G. Autophagy in the pathogenesis of disease. Cell 132, 27–42 (2008)

Veal, E. A., Day, A. M. & Morgan, B. A. Hydrogen peroxide sensing and signaling. Mol. Cell 26, 1–14 (2007)

Moore, C. B. et al. NLRX1 is a regulator of mitochondrial antiviral immunity. Nature 451, 573–577 (2008)

Tattoli, I. et al. NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-κB and JNK pathways by inducing reactive oxygen species production. EMBO Rep. 9, 293–300 (2008)

Hayashi, T., Rizzuto, R., Hajnoczky, G. & Su, T. P. MAM: more than just a housekeeper. Trends Cell Biol. 19, 81–88 (2009)

Zhou, R., Tardivel, A., Thorens, B., Choi, I. & Tschopp, J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nature Immunol. 11, 136–140 (2010)

Saxena, G., Chen, J. & Shalev, A. Intracellular shuttling and mitochondrial function of thioredoxin-interacting protein. J. Biol. Chem. 285, 3997–4005 (2010)

Colombini, M. VDAC: the channel at the interface between mitochondria and the cytosol. Mol. Cell. Biochem. 256, 107–115 (2004)

Oliveira, J. M. Nature and cause of mitochondrial dysfunction in Huntington’s disease: focusing on Huntingtin and the striatum. J. Neurochem. 114, 1–12 (2010)

Restivo, N. L., Srivastava, M. D., Schafer, I. A. & Hoppel, C. L. Mitochondrial dysfunction in a patient with crohn disease: possible role in pathogenesis. J. Pediatr. Gastroenterol. Nutr. 38, 534–538 (2004)

Saitoh, T. et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production. Nature 456, 264–268 (2008)

Yamagata, H. et al. Requirement of voltage-dependent anion channel 2 for pro-apoptotic activity of Bax. Oncogene 28, 3563–3572 (2009)

Sato, T. et al. Fas-mediated apoptosome formation is dependent on reactive oxygen species derived from mitochondrial permeability transition in Jurkat cells. J. Immunol. 173, 285–296 (2004)

Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1adaptors ASC and Ipaf. Nature 430, 213–218 (2004)

Martinon, F., Petrilli, V., Mayor, A., Tardivel, A. & Tschopp, J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237–241 (2006)

Domen, J., Cheshier, S. H. & Weissman, I. L. The role of apoptosis in the regulation of hematopoietic stem cells: Overexpression of Bcl-2 increases both their number and repopulation potential. J. Exp. Med. 191, 253–264 (2000)

Wieckowski, M. R., Giorgi, C., Lebiedzinska, M., Duszynski, J. & Pinton, P. Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells. Nature Protocols 4, 1582–1590 (2009)

Didierlaurent, A. et al. Tollip regulates proinflammatory responses to interleukin-1 and lipopolysaccharide. Mol. Cell. Biol. 26, 735–742 (2006)

Papin, S. et al. The SPRY domain of Pyrin, mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1β processing. Cell Death Differ. 14, 1457–1466 (2007)