NLRP3 recruitment by NLRC4 during Salmonella infection

Journal of Experimental Medicine

Volumn 213, Issue 6, 2016, Pages 877-885

  Qu, Yan ^a,b   Misaghi, Shahram ^a   Newton, Kim ^a   Maltzman, Allie ^a   Izrael Tomasevic, Anita ^a   Arnott, David ^a   Dixit, Vishva M ^a  

^a GENENTECH INC   (United States)

^b PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ADAPTOR PROTEIN ASC; CELL PROTEIN; CRYOPYRIN; FLAGELLIN; INFLAMMASOME; INTERLEUKIN 1BETA CONVERTING ENZYME; NOD LIKE RECEPTOR C4 PROTEIN; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; CALCIUM BINDING PROTEIN; IPAF PROTEIN, MOUSE; NLRP3 PROTEIN, MOUSE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BONE MARROW DERIVED MACROPHAGE; CONTROLLED STUDY; ENZYME ACTIVATION; MOUSE; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SALMONELLA ENTERICA SEROVAR TYPHIMURIUM; SALMONELLOSIS; WILD TYPE; AMINO ACID SUBSTITUTION; ANIMAL; BONE MARROW CELL; GENETICS; IMMUNOLOGY; KNOCKOUT MOUSE; MACROPHAGE; METABOLISM; MICROBIOLOGY; MISSENSE MUTATION; PROTEIN DOMAIN;

AMINO ACID SUBSTITUTION; ANIMALS; APOPTOSIS REGULATORY PROTEINS; BONE MARROW CELLS; CALCIUM-BINDING PROTEINS; FLAGELLIN; MACROPHAGES; MICE; MICE, KNOCKOUT; MUTATION, MISSENSE; NLR FAMILY, PYRIN DOMAIN-CONTAINING 3 PROTEIN; PROTEIN DOMAINS; SALMONELLA INFECTIONS; SALMONELLA TYPHIMURIUM;

EID: 84971577029     PISSN: 00221007     EISSN: 15409538     Source Type: Journal    
DOI: 10.1084/jem.20132234     Document Type: Article

References (22)

1. Broz, P., K. Newton, M. Lamkanfi, S. Mariathasan, V.M. Dixit, and D.M. Monack. 2010a. Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella. J. Exp. Med. 207:1745-1755. http://dx.doi.org/10.1084/jem.20100257
2. Broz, P., J. von Moltke, J.W. Jones, R.E. Vance, and D.M. Monack. 2010b. Differential requirement for Caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing. Cell Host Microbe. 8:471-483. http://dx.doi.org/10.1016/j.chom.2010.11.007
3. Diebolder, C.A., E.F. Halff, A.J. Koster, E.G. Huizinga, and R.I. Koning. 2015. Cryoelectron Tomography of the NAIP5/NLRC4 Inflammasome: Implications for NLR Activation. Structure. 23:2349-2357. http://dx.doi.org/10.1016/j.str.2015.10.001
4. Franchi, L., A. Amer, M. Body-Malapel, T.D. Kanneganti, N. Ozören, R. Jagirdar, N. Inohara, P. Vandenabeele, J. Bertin, A. Coyle, et al. 2006. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1beta in salmonella-infected macrophages. Nat. Immunol. 7:576-582. http://dx.doi.org/10.1038/ni1346
5. Hu, Z., C. Yan, P. Liu, Z. Huang, R. Ma, C. Zhang, R. Wang, Y. Zhang, F. Martinon, D. Miao, et al. 2013. Crystal structure of NLRC4 reveals its autoinhibition mechanism. Science. 341:172-175. http://dx.doi.org/10.1126/science.1236381
6. Hu, Z., Q. Zhou, C. Zhang, S. Fan, W. Cheng, Y. Zhao, F. Shao, H.W. Wang, S.F. Sui, and J. Chai. 2015. Structural and biochemical basis for induced self-propagation of NLRC4. Science. 350:399-404. http://dx.doi.org/10.1126/science.aac5489
7. Jones, J.W., N. Kayagaki, P. Broz, T. Henry, K. Newton, K. O'Rourke, S. Chan, J. Dong, Y. Qu, M. Roose-Girma, et al. 2010. Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis. Proc. Natl. Acad. Sci. USA. 107:9771-9776. http://dx.doi.org/10.1073/pnas.1003738107
8. Kayagaki, N., S. Warming, M. Lamkanfi, L. Vande Walle, S. Louie, J. Dong, K. Newton, Y. Qu, J. Liu, S. Heldens, et al. 2011. Non-canonical inflammasome activation targets caspase-11. Nature. 479:117-121. http://dx.doi.org/10.1038/nature10558
9. Kayagaki, N., M.T. Wong, I.B. Stowe, S.R. Ramani, L.C. Gonzalez, S. Akashi-Takamura, K. Miyake, J. Zhang, W.P. Lee, A. Muszynski, et al. 2013. Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science. 341:1246-1249. http://dx.doi.org/10.1126/science.1240248
10. Kofoed, E.M., and R.E. Vance. 2011. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature. 477:592-595. http://dx.doi.org/10.1038/nature10394
11. Lamkanfi, M., and V.M. Dixit. 2009. Inflammasomes: guardians of cytosolic sanctity. Immunol. Rev. 227:95-105. http://dx.doi.org/10.1111/j.1600-065X.2008.00730.x
12. Man, S.M., L.J. Hopkins, E. Nugent, S. Cox, I.M. Glück, P. Tourlomousis, J.A. Wright, P. Cicuta, T.P. Monie, and C.E. Bryant. 2014. Inflammasome activation causes dual recruitment of NLRC4 and NLRP3 to the same macromolecular complex. Proc. Natl. Acad. Sci. USA. 111:7403-7408. http://dx.doi.org/10.1073/pnas.1402911111
13. Mariathasan, S., K. Newton, D.M. Monack, D. Vucic, D.M. French, W.P. Lee, M. Roose-Girma, S. Erickson, and V.M. Dixit. 2004. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature. 430:213-218. http://dx.doi.org/10.1038/nature02664
14. 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. http://dx.doi.org/10.1038/nature04515
15. Martinon, F., V. Pétrilli, A. Mayor, A. Tardivel, and J. Tschopp. 2006. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature. 440:237-241. http://dx.doi.org/10.1038/nature04516
16. Miao, E.A., C.M. Alpuche-Aranda, M. Dors, A.E. Clark, M.W. Bader, S.I. Miller, and A. Aderem. 2006. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf. Nat. Immunol. 7:569-575. http://dx.doi.org/10.1038/ni1344
17. Poyet, J.L., S.M. Srinivasula, M. Tnani, M. Razmara, T. Fernandes-Alnemri, and E.S. Alnemri. 2001. Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1. J. Biol. Chem. 276:28309-28313. http://dx.doi.org/10.1074/jbc.C100250200
18. Qu, Y., S. Misaghi, A. Izrael-Tomasevic, K. Newton, L.L. Gilmour, M. Lamkanfi, S. Louie, N. Kayagaki, J. Liu, L. Kömüves, et al. 2012. Phosphorylation of NLRC4 is critical for inflammasome activation. Nature. 490:539-542. http://dx.doi.org/10.1038/nature11429
19. Sutterwala, F.S., L.A. Mijares, L. Li, Y. Ogura, B.I. Kazmierczak, and R.A. Flavell. 2007. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. J. Exp. Med. 204:3235-3245. http://dx.doi.org/10.1084/jem.20071239
20. Yang, J., Y. Zhao, J. Shi, and F. Shao. 2013. Human NAIP and mouse NAIP1 recognize bacterial type III secretion needle protein for inflammasome activation. Proc. Natl. Acad. Sci. USA. 110:14408-14413. http://dx.doi.org/10.1073/pnas.1306376110
21. Zhang, L., S. Chen, J. Ruan, J. Wu, A.B. Tong, Q. Yin, Y. Li, L. David, A. Lu, W.L. Wang, et al. 2015. Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization. Science. 350:404-409. http://dx.doi.org/10.1126/science.aac5789
22. Zhao, Y., J. Yang, J. Shi, Y.N. Gong, Q. Lu, H. Xu, L. Liu, and F. Shao. 2011. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature. 477:596-600. http://dx.doi.org/10.1038/nature10510