Advances in Nod-like receptors (NLR) biology

Cytokine and Growth Factor Reviews

Volumn 25, Issue 6, 2014, Pages 681-697

  Barbé, François ^a   Douglas, Todd ^a   Saleh, Maya ^a,b  

^a MCGILL UNIVERSITY   (Canada)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

Cell death; Inflammasome; Inflammation; Innate immunity; NLR

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; CLASS 2 TRANSACTIVATOR; CRYOPYRIN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INHIBITOR OF APOPTOSIS PROTEIN 1; INHIBITOR OF APOPTOSIS PROTEIN 2; NLRB PROTEIN; NLRC3 PROTEIN; NLRC4 PROTEIN; NLRC5 PROTEIN; NLRP1 PROTEIN; NLRP10 PROTEIN; NLRP12 PROTEIN; NLRP6 PROTEIN; NLRP7 PROTEIN; NLRX1 PROTEIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PROTEIN BID; RIP2 PROTEIN; STAT5 PROTEIN; STRESS ACTIVATED PROTEIN KINASE; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG; SIGNAL PEPTIDE;

ANTIVIRAL ACTIVITY; AUTOPHAGY; HUMAN; INFLAMMATION; INNATE IMMUNITY; INTERNALIZATION; ION CURRENT; LYMPHOCYTE FUNCTION; LYSOSOME; MITOCHONDRION; NONHUMAN; OLIGOMERIZATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INDUCTION; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW; SIGNAL TRANSDUCTION; T LYMPHOCYTE; ANIMAL; GENETICS; IMMUNOLOGY;

ANIMALS; HUMANS; IMMUNITY, INNATE; INFLAMMATION; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; SIGNAL TRANSDUCTION;

EID: 84918836876     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2014.07.001     Document Type: Review

References (209)

1. Bryant C.E., Monie T.P. Mice, men and the relatives: cross-species studies underpin innate immunity. Open Biol 2012, 2:120015.
2. Martinon F., Burns K., Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 2002, 10:417-426.
3. Ting J.P., Lovering R.C., Alnemri E.S., Bertin J., Boss J.M., Davis B.K., et al. The NLR gene family: a standard nomenclature. Immunity 2008, 28:285-287.
4. Martin B.K., Chin K.C., Olsen J.C., Skinner C.A., Dey A., Ozato K., et al. Induction of MHC class I expression by the MHC class II transactivator CIITA. Immunity 1997, 6:591-600.
5. Steimle V., Otten L.A., Zufferey M., Mach B. Complementation cloning of an MHC class II transactivator mutated in hereditary MHC class II deficiency (or bare lymphocyte syndrome). Cell 1993, 75:135-146.
6. Spilianakis C., Papamatheakis J., Kretsovali A. Acetylation by PCAF enhances CIITA nuclear accumulation and transactivation of major histocompatibility complex class II genes. Mol Cell Biol 2000, 20:8489-8498.
7. Nagarajan U.M., Bushey A., Boss J.M. Modulation of gene expression by the MHC class II transactivator. J Immunol 2002, 169:5078-5088.
8. Sisk T.J., Gourley T., Roys S., Chang C.H. MHC class II transactivator inhibits IL-4 gene transcription by competing with NF-AT to bind the coactivator CREB binding protein (CBP)/p300. J Immunol 2000, 165:2511-2517.
9. Wu X., Kong X., Luchsinger L., Smith B.D., Xu Y. Regulating the activity of class II transactivator by posttranslational modifications: exploring the possibilities. Mol Cell Biol 2009, 29:5639-5644.
10. Zika E., Fauquier L., Vandel L., Ting J.P. Interplay among coactivator-associated arginine methyltransferase 1, CBP, and CIITA in IFN-gamma-inducible MHC-II gene expression. Proc Natl Acad Sci USA 2005, 102:16321-16326.
11. Wright K.L., Ting J.P. Epigenetic regulation of MHC-II and CIITA genes. Trends Immunol 2006, 27:405-412.
12. Howcroft T.K., Raval A., Weissman J.D., Gegonne A., Singer D.S. Distinct transcriptional pathways regulate basal and activated major histocompatibility complex class I expression. Mol Cell Biol 2003, 23:3377-3391.
13. Mahanta S.K., Scholl T., Yang F.C., Strominger J.L. Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein. Proc Natl Acad Sci USA 1997, 94:6324-6329.
14. Kanazawa S., Okamoto T., Peterlin B.M. Tat competes with CIITA for the binding to P-TEFb and blocks the expression of MHC class II genes in HIV infection. Immunity 2000, 12:61-70.
15. Soe K.C., Devaiah B.N., Singer D.S. Transcriptional coactivator CIITA, a functional homolog of TAF1, has kinase activity. Biochim Biophys Acta 2013, 1829:1184-1190.
16. Inohara N., Koseki T., del Peso L., Hu Y., Yee C., Chen S., et al. Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB. J Biol Chem 1999, 274:14560-14567.
17. Ogura Y., Bonen D.K., Inohara N., Nicolae D.L., Chen F.F., Ramos R., et al. A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease. Nature 2001, 411:603-606.
18. Girardin S.E., Boneca I.G., Carneiro L.A., Antignac A., Jehanno M., Viala J., et al. Nod1 detects a unique muropeptide from Gram-negative bacterial peptidoglycan. Science 2003, 300:1584-1587.
19. Tanabe T., Chamaillard M., Ogura Y., Zhu L., Qiu S., Masumoto J., et al. Regulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition. EMBO J 2004, 23:1587-1597.
20. Chamaillard M., Hashimoto M., Horie Y., Masumoto J., Qiu S., Saab L., et al. An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid. Nat Immunol 2003, 4:702-707.
21. Laroui H., Yan Y., Narui Y., Ingersoll S.A., Ayyadurai S., Charania M.A., et al. l-Ala-gamma-d-Glu-meso-diaminopimelic acid (DAP) interacts directly with leucine-rich region domain of nucleotide-binding oligomerization domain 1, increasing phosphorylation activity of receptor-interacting serine/threonine-protein kinase 2 and its interaction with nucleotide-binding oligomerization domain 1. J Biol Chem 2011, 286:31003-31013.
22. Grimes C.L., Ariyananda Lde Z., Melnyk J.E., O'Shea E.K. The innate immune protein Nod2 binds directly to MDP, a bacterial cell wall fragment. J Am Chem Soc 2012, 134:13535-13537.
23. Mo J., Boyle J.P., Howard C.B., Monie T.P., Davis B.K., Duncan J.A. Pathogen sensing by nucleotide-binding oligomerization domain-containing protein 2 (NOD2) is mediated by direct binding to muramyl dipeptide and ATP. J Biol Chem 2012, 287:23057-23067.
24. Coulombe F., Divangahi M., Veyrier F., de Leseleuc L., Gleason J.L., Yang Y., et al. Increased NOD2-mediated recognition of N-glycolyl muramyl dipeptide. J Exp Med 2009, 206:1709-1716.
25. Tattoli I., Travassos L.H., Carneiro L.A., Magalhaes J.G., Girardin S.E. The nodosome: Nod1 and Nod2 control bacterial infections and inflammation. Semin Immunopathol 2007, 29:289-301.
26. Kobayashi K.S., Chamaillard M., Ogura Y., Henegariu O., Inohara N., Nunez G., et al. Nod2-dependent regulation of innate and adaptive immunity in the intestinal tract. Science 2005, 307:731-734.
27. Bertrand M.J., Doiron K., Labbe K., Korneluk R.G., Barker P.A., Saleh M. Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2. Immunity 2009, 30:789-801.
28. Damgaard R.B., Nachbur U., Yabal M., Wong W.W., Fiil B.K., Kastirr M., et al. The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling in inflammation and innate immunity. Mol Cell 2012, 46:746-758.
29. Barnich N., Aguirre J.E., Reinecker H.C., Xavier R., Podolsky D.K. Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-{kappa}B activation in muramyl dipeptide recognition. J Cell Biol 2005, 170:21-26.
30. Lecine P., Esmiol S., Metais J.Y., Nicoletti C., Nourry C., McDonald C., et al. The NOD2-RICK complex signals from the plasma membrane. J Biol Chem 2007, 282:15197-15207.
31. Kufer T.A., Kremmer E., Banks D.J., Philpott D.J. Role for erbin in bacterial activation of Nod2. Infect Immun 2006, 74:3115-3124.
32. Lipinski S., Grabe N., Jacobs G., Billmann-Born S., Till A., Hasler R., et al. RNAi screening identifies mediators of NOD2 signaling: implications for spatial specificity of MDP recognition. Proc Natl Acad Sci USA 2012, 109:21426-21431.
33. Fukazawa A., Alonso C., Kurachi K., Gupta S., Lesser C.F., McCormick B.A., et al. GEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectors. PLoS Pathog 2008, 4:e1000228.
34. Till A., Rosenstiel P., Brautigam K., Sina C., Jacobs G., Oberg H.H., et al. A role for membrane-bound CD147 in NOD2-mediated recognition of bacterial cytoinvasion. J Cell Sci 2008, 121:487-495.
35. Vavricka S.R., Musch M.W., Chang J.E., Nakagawa Y., Phanvijhitsiri K., Waypa T.S., et al. hPepT1 transports muramyl dipeptide, activating NF-kappaB and stimulating IL-8 secretion in human colonic Caco2/bbe cells. Gastroenterology 2004, 127:1401-1409.
36. Ismair M.G., Vavricka S.R., Kullak-Ublick G.A., Fried M., Mengin-Lecreulx D., Girardin S.E. hPepT1 selectively transports muramyl dipeptide but not Nod1-activating muramyl peptides. Can J Physiol Pharmacol 2006, 84:1313-1319.
37. Dalmasso G., Nguyen H.T., Ingersoll S.A., Ayyadurai S., Laroui H., Charania M.A., et al. The PepT1-NOD2 signaling pathway aggravates induced colitis in mice. Gastroenterology 2011, 141:1334-1345.
38. Mukhopadhyay S., Varin A., Chen Y., Liu B., Tryggvason K., Gordon S. SR-A/MARCO-mediated ligand delivery enhances intracellular TLR and NLR function, but ligand scavenging from cell surface limits TLR4 response to pathogens. Blood 2011, 117:1319-1328.
39. Marina-Garcia N., Franchi L., Kim Y.G., Hu Y., Smith D.E., Boons G.J., et al. Clathrin- and dynamin-dependent endocytic pathway regulates muramyl dipeptide internalization and NOD2 activation. J Immunol 2009, 182:4321-4327.
40. Lee J., Tattoli I., Wojtal K.A., Vavricka S.R., Philpott D.J., Girardin S.E. pH-dependent internalization of muramyl peptides from early endosomes enables Nod1 and Nod2 signaling. J Biol Chem 2009, 284:23818-23829.
41. Charriere G.M., Ip W.E., Dejardin S., Boyer L., Sokolovska A., Cappillino M.P., et al. Identification of Drosophila Yin and PEPT2 as evolutionarily conserved phagosome-associated muramyl dipeptide transporters. J Biol Chem 2010, 285:20147-20154.
42. Nakamura N., Lill J.R., Phung Q., Jiang Z., Bakalarski C., de Maziere A., et al. Endosomes are specialized platforms for bacterial sensing and NOD2 signalling. Nature 2014, 509:240-244.
43. Rigaud S., Fondaneche M.C., Lambert N., Pasquier B., Mateo V., Soulas P., et al. XIAP deficiency in humans causes an X-linked lymphoproliferative syndrome. Nature 2006, 444:110-114.
44. Zeissig Y., Petersen B.S., Milutinovic S., Bosse E., Mayr G., Peuker K., et al. XIAP variants in male Crohn's disease. Gut 2014.
45. Tao M., Scacheri P.C., Marinis J.M., Harhaj E.W., Matesic L.E., Abbott D.W. ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways. Curr Biol 2009, 19:1255-1263.
46. Zurek B., Schoultz I., Neerincx A., Napolitano L.M., Birkner K., Bennek E., et al. TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation. PLoS ONE 2012, 7:e41255.
47. Ver Heul A.M., Fowler C.A., Ramaswamy S., Piper R.C. Ubiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2. J Biol Chem 2013, 288:6890-6902.
48. Rosenstiel P., Huse K., Till A., Hampe J., Hellmig S., Sina C., et al. A short isoform of NOD2/CARD15, NOD2-S, is an endogenous inhibitor of NOD2/receptor-interacting protein kinase 2-induced signaling pathways. Proc Natl Acad Sci USA 2006, 103:3280-3285.
49. Kramer M., Boeck J., Reichenbach D., Kaether C., Schreiber S., Platzer M., et al. NOD2-C2 - a novel NOD2 isoform activating NF-kappaB in a muramyl dipeptide-independent manner. BMC Res Notes 2010, 3:224.
50. Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S. Proteasomal degradation of Nod2 protein mediates tolerance to bacterial cell wall components. J Biol Chem 2012, 287:39800-39811.
51. Mohanan V., Grimes C.L. Hsp70 binds to and stabilizes Nod2, an innate immune receptor involved in Crohn's disease. J Biol Chem 2014, 289:18987-18998.
52. Yang L., Tang Z., Zhang H., Kou W., Lu Z., Li X., et al. PSMA7 directly interacts with NOD1 and regulates its function. Cell Physiol Biochem 2013, 31:952-959.
53. Yeretssian G., Correa R.G., Doiron K., Fitzgerald P., Dillon C.P., Green D.R., et al. Non-apoptotic role of BID in inflammation and innate immunity. Nature 2011, 474:96-99.
54. Nachbur U., Vince J.E., O'Reilly L.A., Strasser A., Silke J. Is BID required for NOD signalling?. Nature 2012, 488:E4-E6. discussion E6-8.
55. Yamamoto-Furusho J.K., Barnich N., Xavier R., Hisamatsu T., Podolsky D.K. Centaurin beta1 down-regulates nucleotide-binding oligomerization domains 1- and 2-dependent NF-kappaB activation. J Biol Chem 2006, 281:36060-36070.
56. Clark N.M., Marinis J.M., Cobb B.A., Abbott D.W. MEKK4 sequesters RIP2 to dictate NOD2 signal specificity. Curr Biol 2008, 18:1402-1408.
57. Lecat A., Di Valentin E., Somja J., Jourdan S., Fillet M., Kufer T.A., et al. The c-Jun N-terminal kinase (JNK)-binding protein (JNKBP1) acts as a negative regulator of NOD2 protein signaling by inhibiting its oligomerization process. J Biol Chem 2012, 287:29213-29226.
58. Conde C., Rambout X., Lebrun M., Lecat A., Di Valentin E., Dequiedt F., et al. The inositol phosphatase SHIP-1 inhibits NOD2-induced NF-kappaB activation by disturbing the interaction of XIAP with RIP2. PLoS ONE 2012, 7:e41005.
59. Lipinski S., Till A., Sina C., Arlt A., Grasberger H., Schreiber S., et al. DUOX2-derived reactive oxygen species are effectors of NOD2-mediated antibacterial responses. J Cell Sci 2009, 122:3522-3530.
60. Hampe J., Franke A., Rosenstiel P., Till A., Teuber M., Huse K., et al. A genome-wide association scan of nonsynonymous SNPs identifies a susceptibility variant for Crohn disease in ATG16L1. Nat Genet 2007, 39:207-211.
61. Rioux J.D., Xavier R.J., Taylor K.D., Silverberg M.S., Goyette P., Huett A., et al. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nat Genet 2007, 39:596-604.
62. Travassos L.H., Carneiro L.A., Ramjeet M., Hussey S., Kim Y.G., Magalhaes J.G., et al. Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry. Nat Immunol 2010, 11:55-62.
63. Cooney R., Baker J., Brain O., Danis B., Pichulik T., Allan P., et al. NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation. Nat Med 2010, 16:90-97.
64. Homer C.R., Richmond A.L., Rebert N.A., Achkar J.P., McDonald C. ATG16L1 and NOD2 interact in an autophagy-dependent antibacterial pathway implicated in Crohn's disease pathogenesis. Gastroenterology 2010, 139. 1630-41, 1641.e1-2.
65. Homer C.R., Kabi A., Marina-Garcia N., Sreekumar A., Nesvizhskii A.I., Nickerson K.P., et al. A dual role for receptor-interacting protein kinase 2 (RIP2) kinase activity in nucleotide-binding oligomerization domain 2 (NOD2)-dependent autophagy. J Biol Chem 2012, 287:25565-25576.
66. Lupfer C., Thomas P.G., Anand P.K., Vogel P., Milasta S., Martinez J., et al. Receptor interacting protein kinase 2-mediated mitophagy regulates inflammasome activation during virus infection. Nat Immunol 2013, 14:480-488.
67. Sorbara M.T., Ellison L.K., Ramjeet M., Travassos L.H., Jones N.L., Girardin S.E., et al. The protein ATG16L1 suppresses inflammatory cytokines induced by the intracellular sensors Nod1 and Nod2 in an autophagy-independent manner. Immunity 2013, 39:858-873.
68. Sabbah A., Chang T.H., Harnack R., Frohlich V., Tominaga K., Dube P.H., et al. Activation of innate immune antiviral responses by Nod2. Nat Immunol 2009, 10:1073-1080.
69. Vissers M., Remijn T., Oosting M., de Jong D.J., Diavatopoulos D.A., Hermans P.W., et al. Respiratory syncytial virus infection augments NOD2 signaling in an IFN-beta-dependent manner in human primary cells. Eur J Immunol 2012, 42:2727-2735.
70. Lupfer C., Thomas P.G., Kanneganti T.D. NOD2 dependent DC activation is necessary for innate immunity and optimal CD8+ T cell responses to influenza A virus infection. J Virol 2014.
71. Shaw M.H., Reimer T., Sanchez-Valdepenas C., Warner N., Kim Y.G., Fresno M., et al. T cell-intrinsic role of Nod2 in promoting type 1 immunity to Toxoplasma gondii. Nat Immunol 2009, 10:1267-1274.
72. Caetano B.C., Biswas A., Lima D.S., Benevides L., Mineo T.W., Horta C.V., et al. Intrinsic expression of Nod2 in CD4+ T lymphocytes is not necessary for the development of cell-mediated immunity and host resistance to Toxoplasma gondii. Eur J Immunol 2011, 41:3627-3631.
73. Zanello G., Goethel A., Forster K., Geddes K., Philpott D.J., Croitoru K. Nod2 activates NF-kB in CD4+ T cells but its expression is dispensable for T cell-induced colitis. PLOS ONE 2013, 8:e82623.
74. Lin G.H., Wortzman M.E., Girardin S.E., Philpott D.J., Watts T.H. T cell intrinsic NOD2 is dispensable for CD8 T cell immunity. PLOS ONE 2013, 8:e56014.
75. Conti B.J., Davis B.K., Zhang J., O'Connor W., Williams K.L., Ting J.P. CATERPILLER 16.2 (CLR16.2), a novel NBD/LRR family member that negatively regulates T cell function. J Biol Chem 2005, 280:18375-18385.
76. Schneider M., Zimmermann A.G., Roberts R.A., Zhang L., Swanson K.V., Wen H., et al. The innate immune sensor NLRC3 attenuates Toll-like receptor signaling via modification of the signaling adaptor TRAF6 and transcription factor NF-kappaB. Nat Immunol 2012, 13:823-831.
77. Shiau C.E., Monk K.R., Joo W., Talbot W.S. An anti-inflammatory NOD-like receptor is required for microglia development. Cell Rep 2013, 5:1342-1352.
78. Zhang L., Mo J., Swanson K.V., Wen H., Petrucelli A., Gregory S.M., et al. NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immune signaling induced by the DNA sensor STING. Immunity 2014, 40:329-341.
79. Meissner T.B., Li A., Biswas A., Lee K.H., Liu Y.J., Bayir E., et al. NLR family member NLRC5 is a transcriptional regulator of MHC class I genes. Proc Natl Acad Sci USA 2010, 107:13794-13799.
80. Kuenzel S., Till A., Winkler M., Hasler R., Lipinski S., Jung S., et al. The nucleotide-binding oligomerization domain-like receptor NLRC5 is involved in IFN-dependent antiviral immune responses. J Immunol 2010, 184:1990-2000.
81. Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., et al. NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways. Cell 2010, 141:483-496.
82. Li L., Xu T., Huang C., Peng Y., Li J. NLRC5 mediates cytokine secretion in RAW264.7 macrophages and modulated by the JAK2/STAT3 pathway. Inflammation 2014, 37:835-847.
83. Benko S., Magalhaes J.G., Philpott D.J., Girardin S.E. NLRC5 limits the activation of inflammatory pathways. J Immunol 2010, 185:1681-1691.
84. Kumar H., Pandey S., Zou J., Kumagai Y., Takahashi K., Akira S., et al. NLRC5 deficiency does not influence cytokine induction by virus and bacteria infections. J Immunol 2011, 186:994-1000.
85. Tong Y., Cui J., Li Q., Zou J., Wang H.Y., Wang R.F. Enhanced TLR-induced NF-kappaB signaling and type I interferon responses in NLRC5 deficient mice. Cell Res 2012, 22:822-835.
86. Davis B.K., Roberts R.A., Huang M.T., Willingham S.B., Conti B.J., Brickey W.J., et al. Cutting edge: NLRC5-dependent activation of the inflammasome. J Immunol 2011, 186:1333-1337.
87. Neerincx A., Rodriguez G.M., Steimle V., Kufer T.A. NLRC5 controls basal MHC class I gene expression in an MHC enhanceosome-dependent manner. J Immunol 2012, 188:4940-4950.
88. Yao Y., Wang Y., Chen F., Huang Y., Zhu S., Leng Q., et al. NLRC5 regulates MHC class I antigen presentation in host defense against intracellular pathogens. Cell Res 2012, 22:836-847.
89. Meissner T.B., Li A., Liu Y.J., Gagnon E., Kobayashi K.S. The nucleotide-binding domain of NLRC5 is critical for nuclear import and transactivation activity. Biochem Biophys Res Commun 2012, 418:786-791.
90. Meissner T.B., Liu Y.J., Lee K.H., Li A., Biswas A., van Eggermond M.C., et al. NLRC5 cooperates with the RFX transcription factor complex to induce MHC class I gene expression. J Immunol 2012, 188:4951-4958.
91. Biswas A., Meissner T.B., Kawai T., Kobayashi K.S. Cutting edge: impaired MHC class I expression in mice deficient for Nlrc5/class I transactivator. J Immunol 2012, 189:516-520.
92. Moore C.B., Bergstralh D.T., Duncan J.A., Lei Y., Morrison T.E., Zimmermann A.G., et al. NLRX1 is a regulator of mitochondrial antiviral immunity. Nature 2008, 451:573-577.
93. Arnoult D., Soares F., Tattoli I., Castanier C., Philpott D.J., Girardin S.E. An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix. J Cell Sci 2009, 122:3161-3168.
94. Allen I.C., Moore C.B., Schneider M., Lei Y., Davis B.K., Scull M.A., et al. NLRX1 protein attenuates inflammatory responses to infection by interfering with the RIG-I-MAVS and TRAF6-NF-kappaB signaling pathways. Immunity 2011, 34:854-865.
95. Rebsamen M., Vazquez J., Tardivel A., Guarda G., Curran J., Tschopp J. NLRX1/NOD5 deficiency does not affect MAVS signalling. Cell Death Differ 2011, 18:1387.
96. Soares F., Tattoli I., Wortzman M.E., Arnoult D., Philpott D.J., Girardin S.E. NLRX1 does not inhibit MAVS-dependent antiviral signalling. Innate Immun 2013, 19:438-448.
97. Hong M., Yoon S.I., Wilson I.A. Structure and functional characterization of the RNA-binding element of the NLRX1 innate immune modulator. Immunity 2012, 36:337-347.
98. Xia X., Cui J., Wang H.Y., Zhu L., Matsueda S., Wang Q., et al. NLRX1 negatively regulates TLR-induced NF-kappaB signaling by targeting TRAF6 and IKK. Immunity 2011, 34:843-853.
99. Lei Y., Wen H., Yu Y., Taxman D.J., Zhang L., Widman D.G., et al. The mitochondrial proteins NLRX1 and TUFM form a complex that regulates type I interferon and autophagy. Immunity 2012, 36:933-946.
100. Boyden E.D., Dietrich W.F. Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet 2006, 38:240-244.
101. Kovarova M., Hesker P.R., Jania L., Nguyen M., Snouwaert J.N., Xiang Z., et al. NLRP1-dependent pyroptosis leads to acute lung injury and morbidity in mice. J Immunol 2012, 189:2006-2016.
102. Moayeri M., Sastalla I., Leppla S.H. Anthrax and the inflammasome. Microbes Infect 2012, 14:392-400.
103. Klimpel K.R., Arora N., Leppla S.H. Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol Microbiol 1994, 13:1093-1100.
104. Ali S.R., Timmer A.M., Bilgrami S., Park E.J., Eckmann L., Nizet V., et al. Anthrax toxin induces macrophage death by p38 MAPK inhibition but leads to inflammasome activation via ATP leakage. Immunity 2011, 35:34-44.
105. Levinsohn J.L., Newman Z.L., Hellmich K.A., Fattah R., Getz M.A., Liu S., et al. Anthrax lethal factor cleavage of Nlrp1 is required for activation of the inflammasome. PLoS Pathog 2012, 8:e1002638.
106. Chavarria-Smith J., Vance R.E. Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor. PLoS Pathog 2013, 9:e1003452.
107. Faustin B., Lartigue L., Bruey J.M., Luciano F., Sergienko E., Bailly-Maitre B., et al. Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell 2007, 25:713-724.
108. Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S., Humke E.W., et al. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide. Proc Natl Acad Sci USA 2008, 105:7803-7808.
109. Bruey J.M., Bruey-Sedano N., Luciano F., Zhai D., Balpai R., Xu C., et al. Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by interaction with NALP1. Cell 2007, 129:45-56.
110. Gerlic M., Faustin B., Postigo A., Yu E.C., Proell M., Gombosuren N., et al. Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation. Proc Natl Acad Sci USA 2013, 110:7808-7813.
111. Liao K.C., Mogridge J. Activation of the Nlrp1b inflammasome by reduction of cytosolic ATP. Infect Immun 2013, 81:570-579.
112. Gorfu G., Cirelli K.M., Melo M.B., Mayer-Barber K., Crown D., Koller B.H., et al. Dual role for inflammasome sensors NLRP1 and NLRP3 in murine resistance to Toxoplasma gondii. MBio 2014, 5. e01117-13.
113. Ewald S.E., Chavarria-Smith J., Boothroyd J.C. NLRP1 is an inflammasome sensor for Toxoplasma gondii. Infect Immun 2014, 82:460-468.
114. D'Osualdo A., Weichenberger C.X., Wagner R.N., Godzik A., Wooley J., Reed J.C. CARD8 and NLRP1 undergo autoproteolytic processing through a ZU5-like domain. PLoS ONE 2011, 6:e27396.
115. Finger J.N., Lich J.D., Dare L.C., Cook M.N., Brown K.K., Duraiswami C., et al. Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity. J Biol Chem 2012, 287:25030-25037.
116. Frew B.C., Joag V.R., Mogridge J. Proteolytic processing of Nlrp1b is required for inflammasome activity. PLoS Pathog 2012, 8:e1002659.
117. de Rivero Vaccari J.P., Lotocki G., Alonso O.F., Bramlett H.M., Dietrich W.D., Keane R.W. Therapeutic neutralization of the NLRP1 inflammasome reduces the innate immune response and improves histopathology after traumatic brain injury. J Cereb Blood Flow Metab 2009, 29:1251-1261.
118. Van Opdenbosch N., Gurung P., Vande Walle L., Fossoul A., Kanneganti T.D., Lamkanfi M. Activation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formation. Nat Commun 2014, 5:3209.
119. Sastalla I., Crown D., Masters S.L., McKenzie A., Leppla S.H., Moayeri M. Transcriptional analysis of the three Nlrp1 paralogs in mice. BMC Genomics 2013, 14:188.
120. Im S.S., Yousef L., Blaschitz C., Liu J.Z., Edwards R.A., Young S.G., et al. Linking lipid metabolism to the innate immune response in macrophages through sterol regulatory element binding protein-1a. Cell Metab 2011, 13:540-549.
121. Gerlic M., Croker B.A., Cengia L.H., Moayeri M., Kile B.T., Masters S.L. NLRP1a expression in Srebp-1a-deficient mice. Cell Metab 2014, 19:345-346.
122. Masters S.L., Gerlic M., Metcalf D., Preston S., Pellegrini M., O'Donnell J.A., et al. NLRP1 inflammasome activation induces pyroptosis of hematopoietic progenitor cells. Immunity 2012, 37:1009-1023.
123. Aksentijevich I., Nowak M., Mallah M., Chae J.J., Watford W.T., Hofmann S.R., et al. De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal-onset multisystem inflammatory disease (NOMID): a new member of the expanding family of pyrin-associated autoinflammatory diseases. Arthritis Rheum 2002, 46:3340-3348.
124. Feldmann J., Prieur A.M., Quartier P., Berquin P., Certain S., Cortis E., et al. Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. Am J Hum Genet 2002, 71:198-203.
125. Juliana C., Fernandes-Alnemri T., Kang S., Farias A., Qin F., Alnemri E.S. Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem 2012, 287:36617-36622.
126. Fernandes-Alnemri T., Kang S., Anderson C., Sagara J., Fitzgerald K.A., Alnemri E.S. Cutting edge: TLR signaling licenses IRAK1 for rapid activation of the NLRP3 inflammasome. J Immunol 2013, 191:3995-3999.
127. Ghonime M.G., Shamaa O.R., Das S., Eldomany R.A., Fernandes-Alnemri T., Alnemri E.S., et al. Inflammasome priming by lipopolysaccharide is dependent upon ERK signaling and proteasome function. J Immunol 2014, 192:3881-3888.
128. Lin K.M., Hu W., Troutman T.D., Jennings M., Brewer T., Li X., et al. IRAK-1 bypasses priming and directly links TLRs to rapid NLRP3 inflammasome activation. Proc Natl Acad Sci USA 2014, 111:775-780.
129. Zhou R., Yazdi A.S., Menu P., Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature 2011, 469:221-225.
130. Bauernfeind F., Bartok E., Rieger A., Franchi L., Nunez G., Hornung V. Cutting edge reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol 2011, 187:613-617.
131. Py B.F., Kim M.S., Vakifahmetoglu-Norberg H., Yuan J. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol Cell 2013, 49:331-338.
132. Shi C.S., Shenderov K., Huang N.N., Kabat J., Abu-Asab M., Fitzgerald K.A., et al. Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction. Nat Immunol 2012, 13:255-263.
133. Hernandez-Cuellar E., Tsuchiya K., Hara H., Fang R., Sakai S., Kawamura I., et al. Cutting edge: nitric oxide inhibits the NLRP3 inflammasome. J Immunol 2012, 189:5113-5117.
134. Mishra B.B., Rathinam V.A., Martens G.W., Martinot A.J., Kornfeld H., Fitzgerald K.A., et al. Nitric oxide controls the immunopathology of tuberculosis by inhibiting NLRP3 inflammasome-dependent processing of IL-1beta. Nat Immunol 2013, 14:52-60.
135. Hara H., Tsuchiya K., Kawamura I., Fang R., Hernandez-Cuellar E., Shen Y., et al. Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity. Nat Immunol 2013, 14:1247-1255.
136. Martinon F., Petrilli V., Mayor A., Tardivel A., Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 2006, 440:237-241.
137. Mariathasan S., Weiss D.S., Newton K., McBride J., O'Rourke K., Roose-Girma M., et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 2006, 440:228-232.
138. Cassel S.L., Eisenbarth S.C., Iyer S.S., Sadler J.J., Colegio O.R., Tephly L.A., et al. The Nalp3 inflammasome is essential for the development of silicosis. Proc Natl Acad Sci USA 2008, 105:9035-9040.
139. Hornung V., Bauernfeind F., Halle A., Samstad E.O., Kono H., Rock K.L., et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol 2008, 9:847-856.
140. Halle A., Hornung V., Petzold G.C., Stewart C.R., Monks B.G., Reinheckel T., et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol 2008, 9:857-865.
141. Craven R.R., Gao X., Allen I.C., Gris D., Bubeck Wardenburg J., McElvania-Tekippe E., et al. Staphylococcus aureus alpha-hemolysin activates the NLRP3-inflammasome in human and mouse monocytic cells. PLoS ONE 2009, 4:e7446.
142. Eisenbarth S.C., Colegio O.R., O'Connor W., Sutterwala F.S., Flavell R.A. Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants. Nature 2008, 453:1122-1126.
143. Duewell P., Kono H., Rayner K.J., Sirois C.M., Vladimer G., Bauernfeind F.G., et al. NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals. Nature 2010, 466:652.
144. Petrilli V., Papin S., Dostert C., Mayor A., Martinon F., Tschopp J. Activation of the NALP3 inflammasome is triggered by low intracellular potassium. Cell Death Differ 2007, 14:1583-1589.
145. Lamkanfi M., Mueller J.L., Vitari A.C., Misaghi S., Fedorova A., Deshayes K., et al. Glyburide inhibits the cryopyrin/Nalp3 inflammasome. J Cell Biol 2009, 187:61-70.
146. Munoz-Planillo R., Kuffa P., Martinez-Colon G., Smith B.L., Rajendiran T.M., Nunez G. K(+) efflux is the common trigger of NLRP3 inflammasome activation by bacterial toxins and particulate matter. Immunity 2013, 38:1142-1153.
147. Lee G.S., Subramanian N., Kim A.I., Aksentijevich I., Goldbach-Mansky R., Sacks D.B., et al. The calcium-sensing receptor regulates the NLRP3 inflammasome through Ca2+ and cAMP. Nature 2012, 492:123-127.
148. Rossol M., Pierer M., Raulien N., Quandt D., Meusch U., Rothe K., et al. Extracellular Ca2+ is a danger signal activating the NLRP3 inflammasome through G protein-coupled calcium sensing receptors. Nat Commun 2012, 3:1329.
149. Compan V., Baroja-Mazo A., Lopez-Castejon G., Gomez A.I., Martinez C.M., Angosto D., et al. Cell volume regulation modulates NLRP3 inflammasome activation. Immunity 2012, 37:487-500.
150. Zhong Z., Zhai Y., Liang S., Mori Y., Han R., Sutterwala F.S., et al. TRPM2 links oxidative stress to NLRP3 inflammasome activation. Nat Commun 2013, 4:1611.
151. Triantafilou K., Hughes T.R., Triantafilou M., Morgan B.P. The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation. J Cell Sci 2013, 126:2903-2913.
152. Martinon F. Signaling by ROS drives inflammasome activation. Eur J Immunol 2010, 40:616-619.
153. Zhou R., Tardivel A., Thorens B., Choi I., Tschopp J. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat Immunol 2010, 11:136-140.
154. Huang H., Hu X., Eno C.O., Zhao G., Li C., White C. An interaction between Bcl-xL and the voltage-dependent anion channel (VDAC) promotes mitochondrial Ca2+ uptake. J Biol Chem 2013, 288:19870-19881.
155. Ichinohe T., Yamazaki T., Koshiba T., Yanagi Y. Mitochondrial protein mitofusin 2 is required for NLRP3 inflammasome activation after RNA virus infection. Proc Natl Acad Sci USA 2013, 110:17963-17968.
156. Bandyopadhyay S., Lane T., Venugopal R., Parthasarathy P.T., Cho Y., Galam L., et al. MicroRNA-133a-1 regulates inflammasome activation through uncoupling protein-2. Biochem Biophys Res Commun 2013, 439:407-412.
157. Shimada K., Crother T.R., Karlin J., Dagvadorj J., Chiba N., Chen S., et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity 2012, 36:401-414.
158. Iyer S.S., He Q., Janczy J.R., Elliott E.I., Zhong Z., Olivier A.K., et al. Mitochondrial cardiolipin is required for Nlrp3 inflammasome activation. Immunity 2013, 39:311-323.
159. Park S., Juliana C., Hong S., Datta P., Hwang I., Fernandes-Alnemri T., et al. The mitochondrial antiviral protein MAVS associates with NLRP3 and regulates its inflammasome activity. J Immunol 2013, 191:4358-4366.
160. Subramanian N., Natarajan K., Clatworthy M.R., Wang Z., Germain R.N. The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell 2013, 153:348-361.
161. Misawa T., Takahama M., Kozaki T., Lee H., Zou J., Saitoh T., et al. Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome. Nat Immunol 2013, 14:454-460.
162. Wang Y., Yang C., Mao K., Chen S., Meng G., Sun B. Cellular localization of NLRP3 inflammasome. Protein Cell 2013, 4:425-431.
163. Lo Y.H., Huang Y.W., Wu Y.H., Tsai C.S., Lin Y.C., Mo S.T., et al. Selective inhibition of the NLRP3 inflammasome by targeting to promyelocytic leukemia protein in mouse and human. Blood 2013, 121:3185-3194.
164. Dowling J.K., Becker C.E., Bourke N.M., Corr S.C., Connolly D.J., Quinn S.R., et al. Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation. J Biol Chem 2014, 289:6429-6437.
165. Bauernfeind F., Rieger A., Schildberg F.A., Knolle P.A., Schmid-Burgk J.L., Hornung V. NLRP3 inflammasome activity is negatively controlled by miR-223. J Immunol 2012, 189:4175-4181.
166. Haneklaus M., Gerlic M., Kurowska-Stolarska M., Rainey A.A., Pich D., McInnes I.B., et al. Cutting edge: miR-223 and EBV miR-BART15 regulate the NLRP3 inflammasome and IL-1beta production. J Immunol 2012, 189:3795-3799.
167. Razmara M., Srinivasula S.M., Wang L., Poyet J.L., Geddes B.J., DiStefano P.S., et al. CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis. J Biol Chem 2002, 277:13952-13958.
168. Ito S., Hara Y., Kubota T. CARD8 is a negative regulator for NLRP3 inflammasome, but mutant NLRP3 in cryopyrin-associated periodic syndromes escapes the restriction. Arthritis Res Ther 2014, 16:R52.
169. Jin J., Yu Q., Han C., Hu X., Xu S., Wang Q., et al. LRRFIP2 negatively regulates NLRP3 inflammasome activation in macrophages by promoting Flightless-I-mediated caspase-1 inhibition. Nat Commun 2013, 4:2075.
170. Labbe K., McIntire C.R., Doiron K., Leblanc P.M., Saleh M. Cellular inhibitors of apoptosis proteins cIAP1 and cIAP2 are required for efficient caspase-1 activation by the inflammasome. Immunity 2011, 35:897-907.
171. Yabal M., Muller N., Adler H., Knies N., Gross C.J., Damgaard R.B., et al. XIAP restricts TNF- and RIP3-dependent cell death and inflammasome activation. Cell Rep 2014, 7:1796-1808.
172. Mitoma H., Hanabuchi S., Kim T., Bao M., Zhang Z., Sugimoto N., et al. The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome. Immunity 2013, 39:123-135.
173. Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundback P., et al. Novel role of PKR in inflammasome activation and HMGB1 release. Nature 2012, 488:670-674.
174. Hett E.C., Slater L.H., Mark K.G., Kawate T., Monks B.G., Stutz A., et al. Chemical genetics reveals a kinase-independent role for protein kinase R in pyroptosis. Nat Chem Biol 2013, 9:398-405.
175. He Y., Franchi L., Nunez G. The protein kinase PKR is critical for LPS-induced iNOS production but dispensable for inflammasome activation in macrophages. Eur J Immunol 2013, 43:1147-1152.
176. Grenier J.M., Wang L., Manji G.A., Huang W.J., Al-Garawi A., Kelly R., et al. Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-kappaB and caspase-1. FEBS Lett 2002, 530:73-78.
177. Elinav E., Strowig T., Kau A.L., Henao-Mejia J., Thaiss C.A., Booth C.J., et al. NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis. Cell 2011, 145:745-757.
178. Dupaul-Chicoine J., Yeretssian G., Doiron K., Bergstrom K.S., McIntire C.R., LeBlanc P.M., et al. Control of intestinal homeostasis, colitis, and colitis-associated colorectal cancer by the inflammatory caspases. Immunity 2010, 32:367-378.
179. Saleh M., Trinchieri G. Innate immune mechanisms of colitis and colitis-associated colorectal cancer. Nat Rev Immunol 2011, 11:9-20.
180. Normand S., Delanoye-Crespin A., Bressenot A., Huot L., Grandjean T., Peyrin-Biroulet L., et al. Nod-like receptor pyrin domain-containing protein 6 (NLRP6) controls epithelial self-renewal and colorectal carcinogenesis upon injury. Proc Natl Acad Sci USA 2011, 108:9601-9606.
181. Wlodarska M., Thaiss C.A., Nowarski R., Henao-Mejia J., Zhang J.P., Brown E.M., et al. NLRP6 inflammasome orchestrates the colonic host-microbial interface by regulating goblet cell mucus secretion. Cell 2014, 156:1045-1059.
182. Anand P.K., Malireddi R.K., Lukens J.R., Vogel P., Bertin J., Lamkanfi M., et al. NLRP6 negatively regulates innate immunity and host defence against bacterial pathogens. Nature 2012, 488:389-393.
183. Kinoshita T., Wang Y., Hasegawa M., Imamura R., Suda T. PYPAF3, a PYRIN-containing APAF-1-like protein, is a feedback regulator of caspase-1-dependent interleukin-1beta secretion. J Biol Chem 2005, 280:21720-21725.
184. Khare S., Dorfleutner A., Bryan N.B., Yun C., Radian A.D., de Almeida L., et al. An NLRP7-containing inflammasome mediates recognition of microbial lipopeptides in human macrophages. Immunity 2012, 36:464-476.
185. Murdoch S., Djuric U., Mazhar B., Seoud M., Khan R., Kuick R., et al. Mutations in NALP7 cause recurrent hydatidiform moles and reproductive wastage in humans. Nat Genet 2006, 38:300-302.
186. Messaed C., Akoury E., Djuric U., Zeng J., Saleh M., Gilbert L., et al. NLRP7, a nucleotide oligomerization domain-like receptor protein, is required for normal cytokine secretion and co-localizes with Golgi and the microtubule-organizing center. J Biol Chem 2011, 286:43313-43323.
187. Wang Y., Hasegawa M., Imamura R., Kinoshita T., Kondo C., Konaka K., et al. PYNOD, a novel Apaf-1/CED4-like protein is an inhibitor of ASC and caspase-1. Int Immunol 2004, 16:777-786.
188. Imamura R., Wang Y., Kinoshita T., Suzuki M., Noda T., Sagara J., et al. Anti-inflammatory activity of PYNOD and its mechanism in humans and mice. J Immunol 2010, 184:5874-5884.
189. Lautz K., Damm A., Menning M., Wenger J., Adam A.C., Zigrino P., et al. NLRP10 enhances Shigella-induced pro-inflammatory responses. Cell Microbiol 2012, 14:1568-1583.
190. Eisenbarth S.C., Williams A., Colegio O.R., Meng H., Strowig T., Rongvaux A., et al. NLRP10 is a NOD-like receptor essential to initiate adaptive immunity by dendritic cells. Nature 2012, 484:510-513.
191. Joly S., Eisenbarth S.C., Olivier A.K., Williams A., Kaplan D.H., Cassel S.L., et al. Cutting edge: Nlrp10 is essential for protective antifungal adaptive immunity against Candida albicans. J Immunol 2012, 189:4713-4717.
192. Williams K.L., Taxman D.J., Linhoff M.W., Reed W., Ting J.P. Cutting edge: monarch-1: a pyrin/nucleotide-binding domain/leucine-rich repeat protein that controls classical and nonclassical MHC class I genes. J Immunol 2003, 170:5354-5358.
193. Williams K.L., Lich J.D., Duncan J.A., Reed W., Rallabhandi P., Moore C., et al. The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals. J Biol Chem 2005, 280:39914-39924.
194. Lich J.D., Williams K.L., Moore C.B., Arthur J.C., Davis B.K., Taxman D.J., et al. Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes. J Immunol 2007, 178:1256-1260.
195. Ye Z., Lich J.D., Moore C.B., Duncan J.A., Williams K.L., Ting J.P. ATP binding by monarch-1/NLRP12 is critical for its inhibitory function. Mol Cell Biol 2008, 28:1841-1850.
196. Arthur J.C., Lich J.D., Aziz R.K., Kotb M., Ting J.P. Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase. J Immunol 2007, 179:6291-6296.
197. Zaki M.H., Vogel P., Malireddi R.K., Body-Malapel M., Anand P.K., Bertin J., et al. The NOD-like receptor NLRP12 attenuates colon inflammation and tumorigenesis. Cancer Cell 2011, 20:649-660.
198. Zaki M.H., Man S.M., Vogel P., Lamkanfi M., Kanneganti T.D. Salmonella exploits NLRP12-dependent innate immune signaling to suppress host defenses during infection. Proc Natl Acad Sci USA 2014, 111:385-390.
199. Vladimer G.I., Weng D., Paquette S.W., Vanaja S.K., Rathinam V.A., Aune M.H., et al. The NLRP12 inflammasome recognizes Yersinia pestis. Immunity 2012, 37:96-107.
200. Zhao Y., Yang J., Shi J., Gong Y.N., Lu Q., Xu H., et al. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 2011, 477:596-600.
201. Franchi L., Amer A., Body-Malapel M., Kanneganti T.D., Ozoren N., Jagirdar R., et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages. Nat Immunol 2006, 7:576-582.
202. Miao E.A., Alpuche-Aranda C.M., Dors M., Clark A.E., Bader M.W., Miller S.I., et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf. Nat Immunol 2006, 7:569-575.
203. Miao E.A., Warren S.E. Innate immune detection of bacterial virulence factors via the NLRC4 inflammasome. J Clin Immunol 2010, 30:502-506.
204. Kofoed E.M., Vance R.E. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 2011, 477:592-595.
205. Tenthorey J.L., Kofoed E.M., Daugherty M.D., Malik H.S., Vance R.E. Molecular basis for specific recognition of bacterial ligands by NAIP/NLRC4 inflammasomes. Mol Cell 2014, 54:17-29.
206. Rayamajhi M., Zak D.E., Chavarria-Smith J., Vance R.E., Miao E.A. Cutting edge: mouse NAIP1 detects the type III secretion system needle protein. J Immunol 2013, 191:3986-3989.
207. Yang J., Zhao Y., Shi J., Shao F. Human NAIP and mouse NAIP1 recognize bacterial type III secretion needle protein for inflammasome activation. Proc Natl Acad Sci USA 2013, 110:14408-14413.
208. Qu Y., Misaghi S., Izrael-Tomasevic A., Newton K., Gilmour L.L., Lamkanfi M., et al. Phosphorylation of NLRC4 is critical for inflammasome activation. Nature 2012, 490:539-542.
209. Suzuki S., Franchi L., He Y., Munoz-Planillo R., Mimuro H., Suzuki T., et al. Shigella type III secretion protein MxiI is recognized by Naip2 to induce Nlrc4 inflammasome activation independently of Pkcdelta. PLoS Pathog 2014, 10:e1003926.