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NOD-Like Receptors: Versatile Cytosolic Sentinels
Abstract
Nucleotide binding oligomerization domain (NOD)-like receptors are cytoplasmic pattern-recognition receptors that together with RIG-I-like receptor (retinoic acid-inducible gene 1), Toll-like receptor (TLR), and C-type lectin families make up the innate pathogen pattern recognition system. There are 22 members of NLRs in humans, 34 in mice, and even a larger number in some invertebrates like sea urchins, which contain more than 200 receptors. Although initially described to respond to intracellular pathogens, NLRs have been shown to play important roles in distinct biological processes ranging from regulation of antigen presentation, sensing metabolic changes in the cell, modulation of inflammation, embryo development, cell death, and differentiation of the adaptive immune response. The diversity among NLR receptors is derived from ligand specificity conferred by the leucine-rich repeats and an NH 2-terminal effector domain that triggers the activation of different biological pathways. Here, we describe NLR genes associated with different biological processes and the molecular mechanisms underlying their function. Furthermore, we discuss mutations in NLR genes that have been associated with human diseases.
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Cites
Gout-associated uric acid crystals activate the NALP3 inflammasome
Martinon, F., Pétrilli, V., Mayor, A., Tardivel, A., & Tschopp, J. (2006) · Nature · doi:10.1038/nature04516 · Cited by 5,326
NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals
Duewell, P., Kono, H., Rayner, K. J., Sirois, C. M., Vladimer, G., Bauernfeind, F. G., Abela, G. S., Franchi, L., Nuñez, G., Schnurr, M., et al. (2010) · Nature · doi:10.1038/nature08938 · Cited by 4,026
Cryopyrin activates the inflammasome in response to toxins and ATP
Mariathasan, S., Weiss, D. S., Newton, K., McBride, J., O'Rourke, K., Roose-Girma, M., Lee, W. P., Weinrauch, Y., Monack, D. M., & Dixit, V. M. (2006) · Nature · doi:10.1038/nature04515 · Cited by 3,080
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658
Non-canonical inflammasome activation targets caspase-11
Kayagaki, N., Warming, S., Lamkanfi, M., Walle, L. V., Louie, S., Dong, J., Newton, K., Qu, Y., Liu, J., Heldens, S., et al. (2011) · Nature · doi:10.1038/nature10558 · Cited by 2,530
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441
The Inflammasomes: Guardians of the Body
Martinon, F., Mayor, A., & Tschopp, J. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132715 · Cited by 2,436
Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
Shimada, K., Crother, T. R., Karlin, J., Dagvadorj, J., Chiba, N., Chen, S., Ramanujan, V. K., Wolf, A. J., Vergnes, L., Ojcius, D. M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.009 · Cited by 2,282
Ghiringhelli, F., Apetoh, L., Tesniere, A., Aymeric, L., Ma, Y., Ortiz, C., Vermaelen, K., Panaretakis, T., Mignot, G., Ullrich, E., et al. (2009) · Nature Medicine · doi:10.1038/nm.2028 · Cited by 1,898
The Inflammasome NLRs in Immunity, Inflammation, and Associated Diseases
Davis, B. K., Wen, H., & Ting, J. P.-Y. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-031210-101405 · Cited by 1,618
Sea Anemone Genome Reveals Ancestral Eumetazoan Gene Repertoire and Genomic Organization
Putnam, N. H., Srivastava, M., Hellsten, U., Dirks, B., Chapman, J., Salamov, A., Terry, A., Shapiro, H., Lindquist, E., Kapitonov, V. V., et al. (2007) · Science · doi:10.1126/science.1139158 · Cited by 1,555
Crucial role for the Nalp3 inflammasome in the immunostimulatory properties of aluminium adjuvants
Eisenbarth, S. C., Colegio, O. R., O’Connor, W., Sutterwala, F. S., & Flavell, R. A. (2008) · Nature · doi:10.1038/nature06939 · Cited by 1,542
Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
Pétrilli, V, Papin, S., Dostert, C., Mayor, A., Martinon, F., & Tschopp, J. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402195 · Cited by 1,445
Travassos, L. H., Carneiro, L. A. M., Ramjeet, M., Hussey, S., Kim, Y.-G., Magalhães, J. G., Yuan, L., Soares, F., Chea, E., Le Bourhis, L., et al. (2010) · Nature Immunology · doi:10.1038/ni.1823 · Cited by 1,306
Self-citationFranchi, L., Amer, A., Body-Malapel, M., Kanneganti, T.-D., Özören, N., Jagirdar, R., Inohara, N., Vandenabeele, P., Bertin, J., Coyle, A., et al. (2006) · Nature Immunology · doi:10.1038/ni1346 · Cited by 1,131
Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
Miao, E. A., Alpuche-Aranda, C. M., Dors, M., Clark, A. E., Bader, M. W., Miller, S. I., & Aderem, A. (2006) · Nature Immunology · doi:10.1038/ni1344 · Cited by 1,127
Sutterwala, F. S., Ogura, Y., Szczepanik, M., Lara-Tejero, M., Lichtenberger, G. S., Grant, E. P., Bertin, J., Coyle, A. J., Galán, J. E., Askenase, P. W., et al. (2006) · Immunity · doi:10.1016/j.immuni.2006.02.004 · Cited by 980
Allen, I. C., TeKippe, E. M., Woodford, R.-M. T., Uronis, J. M., Holl, E. K., Rogers, A. B., Herfarth, H. H., Jobin, C., & Ting, J. P.-Y. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100050 · Cited by 826
Autophagy Controls IL-1β Secretion by Targeting Pro-IL-1β for Degradation
Harris, J., Hartman, M., Roche, C., Zeng, S. G., O'Shea, A., Sharp, F. A., Lambe, E. M., Creagh, E. M., Golenbock, D. T., Tschopp, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.202911 · Cited by 794
Nod2 is required for the regulation of commensal microbiota in the intestine
Petnicki-Ocwieja, T., Hrncir, T., Liu, Y.-J., Biswas, A., Hudcovic, T., Tlaskalova-Hogenova, H., & Kobayashi, K. S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907722106 · Cited by 564
Yazdi, A. S., Guarda, G., Riteau, N., Drexler, S. K., Tardivel, A., Couillin, I., & Tschopp, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008155107 · Cited by 525
Regulation of Legionella Phagosome Maturation and Infection through Flagellin and Host Ipaf
Amer, A., Franchi, L., Kanneganti, T.-D., Body-Malapel, M., Özören, N., Brady, G., Meshinchi, S., Jagirdar, R., Gewirtz, A., Akira, S., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604933200 · Cited by 453
NLR family member NLRC5 is a transcriptional regulator of MHC class I genes
Meissner, T. B., Li, A., Biswas, A., Lee, K.-H., Liu, Y.-J., Bayir, E., Iliopoulos, D., van den Elsen, P. J., & Kobayashi, K. S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008684107 · Cited by 447
Salcedo, R., Worschech, A., Cardone, M., Jones, Y., Gyulai, Z., Dai, R.-M., Wang, E., Ma, W., Haines, D., O'hUigin, C., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100199 · Cited by 429
Inflammasome-mediated disease animal models reveal roles for innate but not adaptive immunity
Brydges, S. D., Mueller, J. L., McGeough, M. D., Pena, C. A., Misaghi, A., Gandhi, C., Putnam, C. D., Boyle, D. L., Firestein, G. S., Horner, A. A., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.05.005 · Cited by 339
Endosomes are specialized platforms for bacterial sensing and NOD2 signalling
Nakamura, N., Lill, J. R., Phung, Q., Jiang, Z., Bakalarski, C., de Mazière, A., Klumperman, J., Schlatter, M., Delamarre, L., & Mellman, I. (2014) · Nature · doi:10.1038/nature13133 · Cited by 313
Cutting Edge: Candida albicans Hyphae Formation Triggers Activation of the Nlrp3 Inflammasome
Joly, S., Ma, N., Sadler, J. J., Soll, D. R., Cassel, S. L., & Sutterwala, F. S. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901323 · Cited by 296
Nigro, G., Rossi, R., Commere, P.-H., Jay, P., & Sansonetti, P. J. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.05.003 · Cited by 277
The innate immune receptor Nod1 protects the intestine from inflammation-induced tumorigenesis
Chen, G. Y., Shaw, M. H., Redondo, G., & Núñez, G. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-2061 · Cited by 261
Defining the Origins of the NOD-Like Receptor System at the Base of Animal Evolution
Lange, C., Hemmrich, G., Klostermeier, U. C., Lopez-Quintero, J. A., Miller, D. J., Rahn, T., Weiss, Y., Bosch, T. C. G., & Rosenstiel, P. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msq349 · Cited by 150
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Szentirmai, É., Millican, N. S., Massie, A. R., & Kapás, L. (2019) · Scientific Reports · doi:10.1038/s41598-019-43502-1 · Cited by 216
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Liao, Z., & Su, J. (2021) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2021.104131 · Cited by 118
Tørresen, O. K., Brieuc, M. S. O., Solbakken, M. H., Sørhus, E., Nederbragt, A. J., Jakobsen, K. S., Meier, S., Edvardsen, R. B., & Jentoft, S. (2018) · BMC Genomics · doi:10.1186/s12864-018-4616-y · Cited by 46
Metadata
- Authors
- Motta, V., Soares, F., Sun, T., & Philpott, D. J.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2015-01
- Volume
- 95
- Issue
- 1
- Pages
- 149-178
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2312601304
- Cited by
- 353
- References
- 32
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- closed
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