Cutting edge: NLRC5-dependent activation of the inflammasome

Journal of Immunology

Volumn 186, Issue 3, 2011, Pages 1333-1337

  Davis, Beckley K ^a   Roberts, Reid A ^b   Huang, Max T ^a   Willingham, Stephen B ^a,d   Conti, Brian J ^a,e   Brickey, W June ^b   Barker, Brianne R ^a   Kwan, Mildred ^b   Taxman, Debra J ^b   Accavitti Loper, Mary Ann ^c   Duncan, Joseph A ^a,b   Ting, Jenny P Y ^a,b  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^d STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CRYOPYRIN; INFLAMMASOME; INTERLEUKIN 1BETA; NLRC5 PROTEIN; PROCASPASE 1; REGULATOR PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

ARTICLE; BIOCHEMISTRY; CELL DEATH; CONTROLLED STUDY; CYTOKINE PRODUCTION; HEMATOPOIETIC CELL; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; INNATE IMMUNITY; MOLECULAR CLONING; MONOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

ANIMALS; CARRIER PROTEINS; CELL LINE, TRANSFORMED; CELL LINE, TUMOR; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; HUMANS; IMMUNITY, INNATE; INFLAMMASOMES; INTERLEUKIN-18; INTERLEUKIN-1BETA; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LEUCINE; MICE; PROTEIN STRUCTURE, TERTIARY; SHIGELLA FLEXNERI; STAPHYLOCOCCUS AUREUS;

EID: 79251550744     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1003111     Document Type: Article

References (22)

1. Benko, S., J. G. Magalhaes, D. J. Philpott, and S. E. Girardin. 2010. NLRC5 limits the activation of inflammatory pathways. J. Immunol. 185: 1681-1691.
2. Cui, J., L. Zhu, X. Xia, H. Y. Wang, X. Legras, J. Hong, J. Ji, P. Shen, S. Zheng, Z. J. Chen, and R. F.Wang. 2010. NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways. Cell 141: 483-496.
3. Kuenzel, S., A. Till, M. Winkler, R. Häsler, S. Lipinski, S. Jung, J. Grötzinger, H. Fickenscher, S. Schreiber, and P. Rosenstiel. 2010. The nucleotide-binding oligomerization domain-like receptor NLRC5 is involved in IFN-dependent antiviral immune responses. J. Immunol. 184: 1990-2000.
4. Meissner, T. B., A. Li, A. Biswas, K. H. Lee, Y. J. Liu, E. Bayir, D. Iliopoulos, P. J. van den Elsen, and K. S. Kobayashi. 2010. NLR family member NLRC5 is a transcriptional regulator of MHC class I genes. Proc. Natl. Acad. Sci. USA 107: 13794-13799.
5. Neerincx, A., K. Lautz, M. Menning, E. Kremmer, P. Zigrino, M. Hosel, H. Buning, R. Schwarzenbacher, and T. A. Kufer. 2010. A role for the human NLR family member NLRC5 in antiviral responses. J. Biol. Chem. 285: 26223-26232.
6. Craven, R. R., X. Gao, I. C. Allen, D. Gris, J. Bubeck Wardenburg, E. McElvania-Tekippe, J. P. Ting, and J. A. Duncan. 2009. Staphylococcus aureus α-hemolysin activates the NLRP3-inflammasome in human and mouse monocytic cells. PLoS ONE 4: e7446.
7. Willingham, S. B., D. T. Bergstralh, W. O'Connor, A. C. Morrison, D. J. Taxman, J. A. Duncan, S. Barnoy, M. M. Venkatesan, R. A. Flavell, M. Deshmukh, et al. 2007. Microbial pathogen-induced necrotic cell death mediated by the inflammasome components CIAS1/cryopyrin/NLRP3 and ASC. Cell Host Microbe 2: 147-159.
8. Ting, J. P., and B. K. Davis. 2005. CATERPILLER: a novel gene family important in immunity, cell death, and diseases. Annu. Rev. Immunol. 23: 387-414.
9. Netea, M. G., C. A. Nold-Petry, M. F. Nold, L. A. Joosten, B. Opitz, J. H. van der Meer, F. L. van de Veerdonk, G. Ferwerda, B. Heinhuis, I. Devesa, et al. 2009. Differential requirement for the activation of the inflammasome for processing and release of IL-1β in monocytes and macrophages. Blood 113: 2324-2335.
10. Martinon, F., A. Mayor, and J. Tschopp. 2009. The inflammasomes: guardians of the body. Annu. Rev. Immunol. 27: 229-265.
11. Mariathasan, S., D. S. Weiss, K. Newton, J. McBride, K. O'Rourke, M. Roose-Girma, W. P. Lee, Y. Weinrauch, D. M. Monack, and V. M. Dixit. 2006. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440: 228-232.
12. Muñoz-Planillo, R., L. Franchi, L. S. Miller, and G. Núñez. 2009. A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the Nlrp3 inflammasome. J. Immunol. 183: 3942-3948.
13. Fernandes-Alnemri, T., J. Wu, J. W. Yu, P. Datta, B. Miller, W. Jankowski, S. Rosenberg, J. Zhang, and E. S. Alnemri. 2007. The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation. Cell Death Differ. 14: 1590-1604.
14. Ting, J. P., S. B. Willingham, and D. T. Bergstralh. 2008. NLRs at the intersection of cell death and immunity. Nat. Rev. Immunol. 8: 372-379.
15. Yu, J.W., J. Wu, Z. Zhang, P. Datta, I. Ibrahimi, S. Taniguchi, J. Sagara, T. Fernandes-Alnemri, and E. S. Alnemri. 2006. Cryopyrin and pyrin activate caspase-1, but not NF-κB, via ASC oligomerization. Cell Death Differ. 13: 236-249.
16. Broz, P., K. Newton, M. Lamkanfi, S. Mariathasan, V. M. Dixit, and D. M. Monack. 2010. Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella. J. Exp. Med. 207: 1745-1755.
17. Miao, E. A., D. P. Mao, N. Yudkovsky, R. Bonneau, C. G. Lorang, S. E. Warren, I. A. Leaf, and A. Aderem. 2010. Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome. Proc. Natl. Acad. Sci. USA 107: 3076-3080.
18. Suzuki, T., L. Franchi, C. Toma, H. Ashida, M. Ogawa, Y. Yoshikawa, H. Mimuro, N. Inohara, C. Sasakawa, and G. Nuñez. 2007. Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages. PLoS Pathog. 3: e111.
19. Ting, J. P., J. A. Duncan, and Y. Lei. 2010. How the noninflammasome NLRs function in the innate immune system. Science 327: 286-290.
20. Ogura, Y., D. K. Bonen, N. Inohara, D. L. Nicolae, F. F. Chen, R. Ramos, H. Britton, T. Moran, R. Karaliuskas, R. H. Duerr, et al. 2001. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 411: 603-606.
21. Girardin, S. E., I. G. Boneca, J. Viala, M. Chamaillard, A. Labigne, G. Thomas, D. J. Philpott, and P. J. Sansonetti. 2003. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J. Biol. Chem. 278: 8869-8872.
22. Hsu, L. C., S. R. Ali, S. McGillivray, P. H. Tseng, S. Mariathasan, E. W. Humke, L. Eckmann, J. J. Powell, V. Nizet, V. M. Dixit, and M. Karin. 2008. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1β secretion in response to Bacillus anthracis infection and muramyl dipeptide. Proc. Natl. Acad. Sci. USA 105: 7803-7808.