Cited by 247Inflammasome and immune disordersImmune Response and InflammationNF-κB Signaling Pathways

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The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation

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Rodgers, Mary A., Bowman, James W., Fujita, Hiroaki, Orazio, Nicole, Shi, Mude, Liang, Qiming, Amatya, Rina, Kelly, Thomas J., Iwai, Kazuhiro, Ting, Jenny, Jung, Jae U.·2014·Journal of Experimental Medicine

DOI 10.1084/jem.20132486PMC PMC4076580

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Abstract

Linear ubiquitination is a newly discovered posttranslational modification that is currently restricted to a small number of known protein substrates. The linear ubiquitination assembly complex (LUBAC), consisting of HOIL-1L, HOIP, and Sharpin, has been reported to activate NF-κB–mediated transcription in response to receptor signaling by ligating linear ubiquitin chains to Nemo and Rip1. Despite recent advances, the detailed roles of LUBAC in immune cells remain elusive. We demonstrate a novel HOIL-1L function as an essential regulator of the activation of the NLRP3/ASC inflammasome in primary bone marrow–derived macrophages (BMDMs) independently of NF-κB activation. Mechanistically, HOIL-1L is required for assembly of the NLRP3/ASC inflammasome and the linear ubiquitination of ASC, which we identify as a novel LUBAC substrate. Consequently, we find that HOIL-1L−/− mice have reduced IL-1β secretion in response to in vivo NLRP3 stimulation and survive lethal challenge with LPS. Together, these data demonstrate that linear ubiquitination is required for NLRP3 inflammasome activation, defining the molecular events of NLRP3 inflammasome activation and expanding the role of LUBAC as an innate immune regulator. Furthermore, our observation is clinically relevant because patients lacking HOIL-1L expression suffer from pyogenic bacterial immunodeficiency, providing a potential new therapeutic target for enhancing inflammation in immunodeficient patients.

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The Inflammasome
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066
The Inflammasomes
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475
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
Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
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
Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
Genomic responses in mouse models poorly mimic human inflammatory diseases
Seok, J., Warren, H. S., Cuenca, A. G., Mindrinos, M. N., Baker, H. V., Xu, W., Richards, D. R., McDonald-Smith, G. P., Gao, H., Hennessy, L., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222878110 · Cited by 3,005
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
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
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
Wertz, I. E., O’Rourke, K. M., Zhou, H., Eby, M. T., Aravind, L., Seshagiri, S., Wu, P., Wiesmann, C., Baker, R. T., Boone, D. L., et al. (2004) · Nature · doi:10.1038/nature02794 · Cited by 1,889
Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
Mariathasan, S., Newton, K., Monack, D. M., Vucic, D., French, D. M., Lee, W. P., Roose-Girma, M., Erickson, S. L., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02664 · Cited by 1,864

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Bellenguez, C., Küçükali, F., Jansen, I. E., Kleineidam, L., Moreno-Grau, S., Amin, N., Naj, A. C., Campos-Martin, R., Grenier-Boley, B., Andrade, V., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01024-z · Cited by 2,498
Targeting the NLRP3 inflammasome in inflammatory diseases
Mangan, M. S. J., Olhava, E. J., Roush, W. R., Seidel, H. M., Glick, G. D., & Latz, E. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.97 · Cited by 1,885
Molecular mechanisms regulating NLRP3 inflammasome activation
Jo, E.-K., Kim, J. K., Shin, D.-M., & Sasakawa, C. (2016) · Cellular & Molecular Immunology · doi:10.1038/cmi.2015.95 · Cited by 1,378
Regulation of inflammasome activation
Man, S. M., & Kanneganti, T. (2015) · Immunological Reviews · doi:10.1111/imr.12296 · Cited by 1,088
Initiation and perpetuation of NLRP 3 inflammasome activation and assembly
Elliott, E. I., & Sutterwala, F. S. (2015) · Immunological Reviews · doi:10.1111/imr.12286 · Cited by 821
Role of pyroptosis in inflammation and cancer
Xiang, W. D., Xie, F., Zhou, X., Wu, Y., Yan, H., Liu, T., Huang, J. S., Wang, F., Zhou, F., & Zhang, L. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00905-x · Cited by 728
Post-Translational Modification Control of Innate Immunity
Liu, J., Qian, C., & Cao, X. (2016) · Immunity · doi:10.1016/j.immuni.2016.06.020 · Cited by 641
Ubiquitination in the regulation of inflammatory cell death and cancer
Cockram, P. E., Kist, M., Prakash, S., Chen, S., Wertz, I. E., & Vucic, D. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00708-5 · Cited by 536
The role of mitochondria in NLRP3 inflammasome activation
Liu, Q., Zhang, D., Hu, D., Zhou, X., & Zhou, Y. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.09.010 · Cited by 475
The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
Song, H., Liu, B., Huai, W., Yu, Z., Wang, W., Zhao, J., Han, L., Jiang, G., Zhang, L., Gao, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13727 · Cited by 466
Inflammasome activation and assembly at a glance
Malik, A., & Kanneganti, T. (2017) · Journal of Cell Science · doi:10.1242/jcs.207365 · Cited by 459
Mitochondria in innate immune signaling
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Magupalli, V. G., Negro, R., Tian, Y., Hauenstein, A. V., Caprio, G. D., Skillern, W., Deng, Q., Ørning, P., Alam, H. B., Maliga, Z., et al. (2020) · Science · doi:10.1126/science.aas8995 · Cited by 392
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Dráber, P., Kupka, S., Reichert, M., Draberova, H., Lafont, É., de Miguel, D., Spilgies, L. M., Šurinová, S., Taraborrelli, L., Hartwig, T., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.009 · Cited by 295
Biallelic hypomorphic mutations in a linear deubiquitinase define otulipenia, an early-onset autoinflammatory disease
Zhou, Q., Yu, X., Demirkaya, E., Deuitch, N. T., Stone, D. L., Tsai, W. L., Kuehn, H. S., Wang, H., Yang, D., Park, Y. H., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612594113 · Cited by 280
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Duong, B. H., Onizawa, M., Osés-Prieto, J. A., Advincula, R., Burlingame, A. L., Malynn, B. A., & Ma, A. I. (2015) · Immunity · doi:10.1016/j.immuni.2014.12.031 · Cited by 275
AIM2 and NLRC4 inflammasomes contribute with ASC to acute brain injury independently of NLRP3
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NLRP3 inflammasome priming: A riddle wrapped in a mystery inside an enigma
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Inflammasomes as therapeutic targets in human diseases
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Han, S., Lear, T., Jerome, J. A., Rajbhandari, S., Snavely, C. A., Gulick, D. L., Gibson, K. F., Zou, C., Chen, B. B., & Mallampalli, R. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645549 · Cited by 207
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Molecular mechanisms of inflammasome signaling
Mathur, A., Hayward, J. A., & Man, S. M. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.3mr0617-250r · Cited by 192
The E3 ubiquitin ligase Pellino2 mediates priming of the NLRP3 inflammasome
Humphries, F., Bergin, R., Jackson, R. P., Delagic, N., Wang, B., Yang, S., Dubois, A. V., Ingram, R. J., & Moynagh, P. N. (2018) · Nature Communications · doi:10.1038/s41467-018-03669-z · Cited by 197
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Thaiss, C. A., Levy, M., Itav, S., & Elinav, E. (2016) · Trends in Immunology · doi:10.1016/j.it.2015.12.003 · Cited by 189
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Gorp, H. V., Saavedra, P. H. V., de Vasconcelos, N. M., Opdenbosch, N. V., Walle, L. V., Matusiak, M., Prencipe, G., Insalaco, A., Hauwermeiren, F. V., Demon, D., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613156113 · Cited by 185
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Control of the inflammasome by the ubiquitin system
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Pyroptosis and Its Role in Autoimmune Disease: A Potential Therapeutic Target
You, R., He, X., Zeng, Z., Zhan, Y., Xiao, Y., & Xiao, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.841732 · Cited by 150
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The ubiquitin system: a critical regulator of innate immunity and pathogen–host interactions
Li, J., Chai, Q., & Liu, C. H. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.40 · Cited by 117
Regulation of the linear ubiquitination of STAT1 controls antiviral interferon signaling
Zuo, Y., Feng, Q., Jin, L., Huang, F., Miao, Y., Liu, J., Xu, Y., Chen, X., Zhang, H., Guo, T., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14948-z · Cited by 115
Roles of linear ubiquitinylation, a crucial regulator of NF ‐κB and cell death, in the immune system
Sasaki, K., & Iwaï, K. (2015) · Immunological Reviews · doi:10.1111/imr.12308 · Cited by 115
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Gupta, S., Cassel, S. L., Sutterwala, F. S., & Dagvadorj, J. (2024) · Immunological Reviews · doi:10.1111/imr.13410 · Cited by 116
Stressing out the mitochondria: Mechanistic insights into NLRP3 inflammasome activation
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The intra‐ and extracellular functions of ASC specks
Franklin, B. S., Latz, E., & Schmidt, F. I. (2017) · Immunological Reviews · doi:10.1111/imr.12611 · Cited by 112
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Perception of self: distinguishing autoimmunity from autoinflammation
van Kempen, T. S., Wenink, M. H., Leijten, E. F. A., Radstake, T. R. D. J., & Boes, M. L. (2015) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2015.60 · Cited by 108
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Erlich, Z., Shlomovitz, I., Edry‐Botzer, L., Cohen, H., Frank, D. O., Wang, H., Lew, A. M., Lawlor, K. E., Zhan, Y., Vince, J. E., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0313-5 · Cited by 100
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Gao, J., Liu, R. T., Cao, S., Cui, J. Z., Wang, A., To, E. C., & Matsubara, J. A. (2015) · Mediators of Inflammation · doi:10.1155/2015/690243 · Cited by 105
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Ley, K. F., Pramod, A. B., Croft, M., Ravichandran, K. S., & Ting, J. P. ‐. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00204 · Cited by 101
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Rittinger, K., & Ikeda, F. (2017) · Open Biology · doi:10.1098/rsob.170026 · Cited by 101
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Guo, Y., Li, L., Xu, T., Guo, X., Wang, C., Li, Y., Yang, Y., Yang, D., Sun, B., Zhao, X., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci138234 · Cited by 96
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Shim, D.-W., Shin, W.-Y., Yu, S., Kim, B.-H., Ye, S.-K., Koppula, S., Won, H., Kang, T., & Lee, K.-H. (2017) · Scientific Reports · doi:10.1038/s41598-017-15314-8 · Cited by 91
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Authors: Rodgers, M. A., Bowman, J. W., Fujita, H., Orazio, N., Shi, M., Liang, Q., Amatya, R., Kelly, T. J., Iwai, K., Ting, J., & Jung, J. U.
Affiliations: University of Southern California (US)
Kyoto University (JP)
Department of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan 2
University of North Carolina at Chapel Hill (US)
Corresponding author: Jung, Jae U.
ORCID: Rodgers, Mary A.
Bowman, James W.
Fujita, Hiroaki
Orazio, Nicole
Liang, Qiming
Amatya, Rina
Kelly, Thomas J.
Ting, Jenny
Jung, Jae U.
Venue: Journal of Experimental Medicine
Publisher: Rockefeller University Press
Published: 2014-06-23
Volume: 211
Issue: 7
Pages: 1333-1347
ISSN: 0022-1007 (ISSN-L)
1540-9538
DOI: 10.1084/jem.20132486
PMC: PMC4076580
OpenAlex: W2139206194
Cited by: 247
References: 62
Citations by year: 2026: 10 · 2025: 10 · 2024: 14 · 2023: 20 · 2022: 17 · 2021: 23 · 2020: 18 · 2019: 22 · 2018: 22 · 2017: 29 · 2016: 31 · 2015: 27 · 2014: 4
FWCI: 12.43
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Experimental Medicine (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
UNC Libraries
Funders: National Institutes of Health (1s10rr022508-01a1, 1f32ai096698-01)
Japan Society for the Promotion of Science (24112002)
National Heart, Lung, and Blood Institute (HL110609, R01HL110609)
National Cancer Institute (R01CA156330, CA180779, CA082057, P01CA180779, CA-31363, R01CA082057, CA115284, CA156330, R01CA031363, R01CA115284)
National Institute of Allergy and Infectious Diseases (AI073099, 1F32AI096698, R01AI073099, R37AI029564, F32-AI096698, U19AI083025, R56AI029564, AI083025, AI029564, R01AI029564)
National Institute of Diabetes and Digestive and Kidney Diseases (P30DK048522)
National Center for Research Resources (S10-RR022508)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: LUBAC, linear ubiquitination, NLRP3 inflammasome, ASC, HOIL-1L, macrophages, IL-1β secretion, innate immunity, post-translational modification
MeSH terms: NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Carrier Proteins, Humans, Immunity, Innate, Lipopolysaccharides, Macrophages, NF-kappa B, Common Variable Immunodeficiency, Mice, Knockout, GTPase-Activating Proteins, Ubiquitin-Protein Ligases, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Mice, Interleukin-1beta, Ubiquitination, Inflammasomes

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The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation

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