IAPs limit activation of RIP kinases by TNF receptor 1 during development
Open accessAbstract
Inhibitor of apoptosis (IAP) proteins cIAP1, cIAP2, and XIAP (X-linked IAP) regulate apoptosis and cytokine receptor signalling, but their overlapping functions make it difficult to distinguish their individual roles. To do so, we deleted the genes for IAPs separately and in combination. While lack of any one of the IAPs produced no overt phenotype in mice, deletion of cIap1 with cIap2 or Xiap resulted in mid-embryonic lethality. In contrast, Xiap(-/-)cIap2(-/-) mice were viable. The death of cIap2(-/-)cIap1(-/-) double mutants was rescued to birth by deletion of tumour necrosis factor (TNF) receptor 1, but not TNFR2 genes. Remarkably, hemizygosity for receptor-interacting protein kinase 1 (Ripk1) allowed Xiap(-/-)cIap1(-/-) double mutants to survive past birth, and prolonged cIap2(-/-)cIap1(-/-) embryonic survival. Similarly, deletion of Ripk3 was able to rescue the mid-gestation defect of cIap2(-/-)cIap1(-/-) embryos, as these embryos survived to E15.5. cIAPs are therefore required during development to limit activity of RIP kinases in the TNF receptor 1 signalling pathway.
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Necroptosis is tonically inhibited by c-IAPs, owing to their ability to ubiquitinate RIPK1.
“Necroptosis is also tonically inhibited by c-IAPs, owing to their ability to ubiquitinate RIPK1 [490–493].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [491]
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Shared Principles in NF-κB Signaling
Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,814 · see citing works
Manipulating the mouse embryo: A laboratory manual
Hogan, B., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,467 · see citing works
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738 · see citing works
Manipulating the mouse embryo: A laboratory manual
Johnson, M. (1986) · Trends in Genetics · doi:10.1016/0168-9525(86)90275-1 · Cited by 2,259 · see citing works
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059 · see citing works
Varfolomeev, E., Schuchmann, M., Luria, V., Chiannilkulchai, N., Beckmann, J., Mett, I., Rebrikov, D., Brodianski, V. M., Kemper, O., Kollet, O., et al. (1998) · Immunity · doi:10.1016/s1074-7613(00)80609-3 · Cited by 1,332 · see citing works
Schwenk, F., Baron, U., & Rajewsky, K. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.24.5080 · Cited by 1,289 · see citing works
Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278 · cited 2× · see citing works
“…of Fadd null embryos to birth (Zhang et al , 2011), and deletion of RIPK3, which is thought to act downstream of RIPK1 in the necroptotic pathway, was shown to allow Casp8 KO mice to develop into normal, fertile adults (Ch’en et al , 2011; Kaiser et al , 2011; Oberst et al , 2011) (Figure 8A).”
IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNFα-Dependent Apoptosis
Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218 · see citing works
High-efficiency deleter mice show that FLPe is an alternative to Cre-loxP
Rodríguez, C. I., Buchholz, F., Galloway, J. L., Sequerra, R., Kasper, J. S., Ayala, R., Stewart, A. F., & Dymecki, S. M. (2000) · Nature Genetics · doi:10.1038/75973 · Cited by 1,162 · see citing works
Bertrand, M. J. M., Milutinovic, S., Dickson, K. M., Ho, W. C., Boudreault, A., Durkin, J. P., Gillard, J. W., Jaquith, J. B., Morris, S. J., & Barker, P. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.014 · Cited by 1,102 · see citing works
IAP Antagonists Target cIAP1 to Induce TNFα-Dependent Apoptosis
Vince, J. E., Wong, W. W.-L., Khan, N. R., Feltham, R., Chau, D., Ahmed, A. U., Benetatos, C. A., Chunduru, S. K., Condon, S. M., McKinlay, M. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.037 · Cited by 1,061 · see citing works
Self-citationRIP3 mediates the embryonic lethality of caspase-8-deficient mice
Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., & Mocarski, E. S. (2011) · Nature · doi:10.1038/nature09857 · Cited by 1,057 · see citing works
Rothe, M., Pan, M.-G., Henzel, W. J., Ayres, T. M., & V. Goeddel, D. (1995) · Cell · doi:10.1016/0092-8674(95)90149-3 · Cited by 1,030 · see citing works
Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes
Listen, P., Roy, N., Tamai, K., Lefebvre, C. A., Baird, S. D., Cherton-Horvat, G., Farahani, R., McLean, M., lkeda, J.-E., MacKenzie, A., et al. (1996) · Nature · doi:10.1038/379349a0 · Cited by 1,005 · see citing works
Hitomi, J., Christofferson, D. E., Ng, A., Yao, J., Degterev, A., Xavier, R. J., & Yuan, J. (2008) · Cell · doi:10.1016/j.cell.2008.10.044 · Cited by 989 · see citing works
FADD: Essential for Embryo Development and Signaling from Some, But Not All, Inducers of Apoptosis
Yeh, W., de la Pompa, J. L., McCurrach, M. E., Shu, H., Elia, A., Shahinian, A., Ng, M. S. W., Wakeham, A. C., Khoo, W., Mitchell, K., et al. (1998) · Science · doi:10.1126/science.279.5358.1954 · Cited by 886 · see citing works
Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family
Eckelman, B. P., Salvesen, G. S., & Scott, F. L. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400795 · Cited by 813 · see citing works
IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer
Gyrd-Hansen, M., & Meier, P. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2889 · Cited by 790 · see citing works
Haas, T. L., Emmerich, C. H., Gerlach, B., Schmukle, A. C., Cordier, S. M., Rieser, E., Feltham, R., Vince, J. E., Warnken, U. H., Wenger, T., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.013 · Cited by 768 · see citing works
Self-citationDuckett, C. S., Nava, V. E., Gedrich, R. W., Clem, R. J., Dongen, J. L. V., Gilfillan, M. C., Shiels, H., Hardwick, J. M., & Thompson, C. B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00629.x · Cited by 633 · see citing works
c-IAP1 and c-IAP2 Are Critical Mediators of Tumor Necrosis Factor α (TNFα)-induced NF-κB Activation
Varfolomeev, E. E., Goncharov, T., Fedorova, A. V., Dynek, J. N., Zobel, K., Deshayes, K., Fairbrother, W. J., & Vucic, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800128200 · Cited by 554 · see citing works
Birnbaum, M. J., Clem, R. J., & Miller, L. K. (1994) · Journal of Virology · doi:10.1128/jvi.68.4.2521-2528.1994 · Cited by 541 · see citing works
Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation
Mahoney, D. J., Cheung, H. H., Mrad, R. L., Plenchette, S., Simard, C., Enwere, E., Arora, V., Mak, T. W., Lacasse, E. C., Waring, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711122105 · Cited by 540 · see citing works
Yeh, W.-C., Itie, A., Elia, A. J., Ng, M., Shu, H.-B., Wakeham, A., Mirtsos, C., Suzuki, N., Bonnard, M., Goeddel, D. V., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)80214-9 · Cited by 515 · see citing works
Uren, A. G., Pakusch, M., Hawkins, C. J., Puls, K. L., & Vaux, D. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4974 · Cited by 511 · see citing works
Self-citationCleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
Feng, S., Yang, Y., Mei, Y., Ma, L., Zhu, D.-E., Höti, N., Castanares, M. A., & Wu, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.05.016 · Cited by 445 · see citing works
Interactions of Tumor Necrosis Factor (TNF) and TNF Receptor Family Members in the Mouse and Human
Bossen, C., Ingold, K., Tardivel, A., Bodmer, J.-L., Gaide, O., Hertig, S., Ambrose, C. M., Tschopp, J., & Schneider, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601553200 · Cited by 443 · see citing works
Functional complementation between FADD and RIP1 in embryos and lymphocytes
Zhang, H., Zhou, X., McQuade, T. J., Li, J., Chan, F. K.-M., & Zhang, J. (2011) · Nature · doi:10.1038/nature09878 · Cited by 422 · see citing works
Characterization of XIAP-Deficient Mice
Harlin, H., Reffey, S. B., Duckett, C. S., Lindsten, T., & Thompson, C. B. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3604-3608.2001 · Cited by 422 · see citing works
Q-VD-OPh, a broad spectrum caspase inhibitor with potent antiapoptotic properties
Caserta, T. M., Smith, A. N., Gultice, A. D., Reedy, M., & Brown, T. L. (2003) · APOPTOSIS · doi:10.1023/a:1024116916932 · Cited by 408 · see citing works
TAK1 is Critical for IκB Kinase-mediated Activation of the NF-κB Pathway
Takaesu, G., Surabhi, R. M., Park, K.-J., Ninomiya‐Tsuji, J., Matsumoto, K., & Gaynor, R. B. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01404-3 · Cited by 404 · see citing works
Targeted disruption of the MHC class II Aa gene in C57BL/6 mice
Köntgen, F., Süss, G., Stewart, C. L., Steinmetz, M., & Bluethmann, H. (1993) · International Immunology · doi:10.1093/intimm/5.8.957 · Cited by 364 · see citing works
Gyrd‐Hansen, M., Darding, M., Miasari, M., Santoro, M. M., Zender, L., Xue, W., Tenev, T., da Fonseca, P. C. A., Zvelebil, M., Bujnicki, J. M., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1789 · Cited by 255 · see citing works
Self-citationCellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment
Geserick, P., Hupe, M., Moulin, M., Wong, W. W.-L., Feoktistova, M., Kellert, B., Gollnick, H. P. M., Silke, J., & Leverkus, M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200904158 · Cited by 244 · see citing works
Self-citationVince, J. E., Chau, D., Callus, B. A., Wong, W. W.-L., Hawkins, C. J., Schneider, P., McKinlay, M. A., Benetatos, C. A., Condon, S. M., Chunduru, S. K., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801010 · Cited by 236 · see citing works
Self-citationMechanisms of necroptosis in T cells
Ch’en, I. L., Tsau, J., Molkentin, J. D., Komatsu, M., & Hedrick, S. Μ. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20110251 · Cited by 229 · see citing works
Inhibitor of Apoptosis Protein cIAP2 Is Essential for Lipopolysaccharide-Induced Macrophage Survival
Conte, D., Holčı́k, M., Lefebvre, C. A., LaCasse, E. C., Picketts, D. J., Wright, K. E., & Korneluk, R. G. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.2.699-708.2006 · Cited by 192 · see citing works
Posttranscriptional Downregulation of c-IAP2 by the Ubiquitin Protein Ligase c-IAP1 In Vivo
Conze, D. B., Albert, L., Ferrick, D. A., Goeddel, D. V., Yeh, W., Mak, T. W., & Ashwell, J. D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.3348-3356.2005 · Cited by 186 · see citing works
Smac Mimetics Activate the E3 Ligase Activity of cIAP1 Protein by Promoting RING Domain Dimerization
Feltham, R., Bettjeman, B., Budhidarmo, R., Mace, P. D., Shirley, S., Condon, S. M., Chunduru, S. K., McKinlay, M. A., Vaux, D. L., Silke, J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.222919 · Cited by 168 · see citing works
Self-citationThomas, T., Voss, A. K., Chowdhury, K., & Gruß, P. (2000) · Development · doi:10.1242/dev.127.12.2537 · Cited by 159 · see citing works
Self-citationIAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms
Tenev, T., Zachariou, A., Wilson, R., Ditzel, M., & Meier, P. (2004) · Nature Cell Biology · doi:10.1038/ncb1204 · Cited by 158 · see citing works
Pastorino, J. G., Tafani, M., & Farber, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.27.19411 · Cited by 140 · see citing works
Nguyen, L. T., Duncan, G. S., Mirtsos, C., Ng, M. S. W., Speiser, D. E., Shahinian, A., Marino, M. W., Mak, T. W., Ohashi, P. S., & Yeh, W. (1999) · Immunity · doi:10.1016/s1074-7613(00)80113-2 · Cited by 136 · see citing works
Birc2 (cIap1) regulates endothelial cell integrity and blood vessel homeostasis
Santoro, M. M., Samuel, T., Mitchell, T. S., Reed, J. C., & Stainier, D. Y. R. (2007) · Nature Genetics · doi:10.1038/ng.2007.8 · Cited by 135 · see citing works
Prevention of Hepatic Apoptosis and Embryonic Lethality in RelA/TNFR-1 Double Knockout Mice
Rosenfeld, M. E., Prichard, L. B., Shiojiri, N., & Fausto, N. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64967-x · Cited by 129 · see citing works
Gardam, S., Turner, V. M., Anderton, H., Limaye, S., Basten, A., Köentgen, F., Vaux, D. L., Silke, J., & Brink, R. A. (2011) · Blood · doi:10.1182/blood-2010-10-312793 · Cited by 104 · see citing works
Self-citationHughes, E. D., Qu, Y. Y., Genik, S. J., Lyons, R. H., Pacheco, C. D., Lieberman, A. P., Samuelson, L. C., Nasonkin, I. O., Camper, S. A., Keuren, M. L. V., et al. (2007) · Mammalian Genome · doi:10.1007/s00335-007-9054-0 · Cited by 65 · see citing works
Feltham, R., Moulin, M., Vince, J. E., Mace, P. D., Wong, W. W.-L., Anderton, H., Day, C. L., Vaux, D. L., & Silke, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.087635 · Cited by 42 · see citing works
Self-citationGenomic Characterization of the Mouse Inhibitor of Apoptosis Protein 1 and 2 Genes
Liston, P., Lefebvre, C. A., Fong, W. G., Xuan, J. Y., & Korneluk, R. G. (1997) · Genomics · doi:10.1006/geno.1997.5059 · Cited by 19 · see citing works
Shafey, D., Korneluk, R. G., & Holčı́k, M. (2006) · APOPTOSIS · doi:10.1007/s10495-006-6985-y · Cited by 2 · see citing works
Flagged first, then by citations
1 of the 52 references couldn’t be matched to a known paper.
Cited by
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Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Self-citationCell Death SignalingPreprint
Green, D. R., & Llambi, F. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006080 · Cited by 1,117 · see citing works
“Consequently, treatments with cIAP1/2 inhibitors or expression of the deubiquitylase CYLD promote TNFR1-induced necrosis (Wang et al. 2008b; O’Donnell et al. 2011; Moulin et al. 2012).”
BackgroundNecroptosis in development, inflammation and disease
Weinlich, R., Oberst, A., Beere, H. M., & Green, D. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.149 · Cited by 1,016 · see citing works
Death by TNF: a road to inflammation
Loo, G., & Bertrand, M. J. M. (2022) · Nature reviews. Immunology · doi:10.1038/s41577-022-00792-3 · Cited by 977 · see citing works
RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL
Lawlor, K. E., Khan, N. R., Mildenhall, A., Gerlic, M., Croker, B. A., D’Cruz, A. A., Hall, C. M., Spall, S. K., Anderton, H., Masters, S. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms7282 · Cited by 643 · see citing works
Self-citationThe diverse role of RIP kinases in necroptosis and inflammation
Silke, J., Rickard, J. A., & Gerlic, M. (2015) · Nature Immunology · doi:10.1038/ni.3206 · Cited by 522 · see citing works
Self-citationUbiquitination 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 520 · see citing works
Chu, W. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.10.014 · Cited by 503 · see citing works
“The normal development of c-IAPs knockout mice, which show embryonic lethality, can be rescued via deletion of TNFR1 but not TNFR2, further indicating a critical role for TNFR1 in TNF-induced apoptosis [8].”
BackgroundMlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis
Wu, J., Huang, Z., Ren, J., Zhang, Z., He, P., Li, Y., Ma, J., Chen, W., Zhang, Y., Zhou, X., et al. (2013) · Cell Research · doi:10.1038/cr.2013.91 · Cited by 452 · see citing works
Dondelinger, Y., Jouan-Lanhouet, S., Divert, T., Theatre, E., Bertin, J., Gough, P. J., Giansanti, P., Heck, A. J. R., Dejardin, E., Vandenabeele, P., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.032 · Cited by 431 · see citing works
Apoptosis, Pyroptosis, and Necroptosis—Oh My! The Many Ways a Cell Can Die
Ketelut-Carneiro, N., & Fitzgerald, K. A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167378 · Cited by 418 · see citing works
Newton, K., & Manning, G. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014830 · Cited by 401 · see citing works
Mitochondria-mediated apoptosis in mammals
Xiong, S., Mu, T., Wang, G., & Jiang, X. (2014) · Protein & Cell · doi:10.1007/s13238-014-0089-1 · Cited by 400 · see citing works
“…with XIAP deletion are normal and have no detectable defect in apoptosis with a compensating up-regulation of c-IAP1 and c-IAP2 (Harlin et al., 2001), while mice with deletion of cIAP1 in combination with cIAP2 or XIAP show embryonic lethality due to cardiovascular defects (Moulin et al., 2012).”
Apoptotic cell death in disease—Current understanding of the NCCD 2023
Vitale, I., Pietrocola, F., Guilbaud, E., Aaronson, S. A., Abrams, J., Adam, D., Agostini, M., Agostinis, P., Alnemri, E. S., Altucci, L., et al. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01153-w · Cited by 359 · see citing works
RIP3: a molecular switch for necrosis and inflammationPreprint
Moriwaki, K., & Chan, F. K.-M. (2013) · Genes & Development · doi:10.1101/gad.223321.113 · Cited by 353 · see citing works
“5 (Moulin et al. 2012).”
BackgroundInfluentialProgrammed Necrosis in the Cross Talk of Cell Death and Inflammation
Chan, F. K.-M., Luz, N. F., & Moriwaki, K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032414-112248 · Cited by 350 · see citing works
“The importance of cIAPs and the ubiquitin machinery in regulating RIPK activities and necroptosis is illustrated by the partial rescue of embryonic lethality of ciap1−/−xiap−/− or ciap1−/−ciap2−/− embryos by loss of Ripk3 or a single Ripk1 allele (18).”
BackgroundMutations that prevent caspase cleavage of RIPK1 cause autoinflammatory disease
Lalaoui, N., Boyden, S. E., Oda, H., Wood, G., Stone, D. L., Chau, D., Liu, L., Stoffels, M., Kratina, T., Lawlor, K. E., et al. (2019) · Nature · doi:10.1038/s41586-019-1828-5 · Cited by 331 · see citing works
“This phenotype was reminiscent of several strains of knock-out mice with defects in TNF signalling, including Casp8 -/- mice 8,16–22 .”
Self-citationInhibitor of Apoptosis (IAP) Proteins-Modulators of Cell Death and InflammationPreprint
Silke, J., & Meier, P. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008730 · Cited by 329 · see citing works
“Embryonic lethality is also partially rescued by crossing the XiapClap1 and Clap1 Clap2 mice to Ripk1 and Ripk3 mice (Moulin et al. 2012), showing that these IAPs function together as critical regulators of an embryonic decision point involving RIP kinase activity.”
BackgroundInfluentialSelf-citationCell death pathways: intricate connections and disease implications
Kist, M., & Vucic, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020106700 · Cited by 328 · see citing works
“…in complex I with K11-and K63-linked ubiquitin chains (Bertrand et al , 2008; Mahoney et al , 2008; Varfolomeev et al , 2008; Dynek et al , 2010; Moulin et al , 2012), resulting in LUBAC (linear ubiquitin chain assembly complex) recruitment, and addition of linear ubiquitin chains (Haas et al ,…”
Webster, J. D., & Vucic, D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00365 · Cited by 315 · see citing works
Dondelinger, Y., Aguileta, M. A., Goossens, V, Dubuisson, C., Grootjans, S., Dejardin, E., Vandenabeele, P., & Bertrand, M. J. M. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.94 · Cited by 312 · see citing works
“12,13 16 Consequently, their depletion, obtained either genetically or by the use of Smac Mimetics (SM), also induces a switch to apoptosis.”
Roles of Caspases in Necrotic Cell Death
Yuan, J., Najafov, A., & Py, B. F. (2016) · Cell · doi:10.1016/j.cell.2016.11.047 · Cited by 290 · see citing works
Checkpoints in TNF-Induced Cell Death: Implications in Inflammation and Cancer
Annibaldi, A., & Meier, P. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.11.002 · Cited by 287 · see citing works
XIAP Restricts TNF- and RIP3-Dependent Cell Death and Inflammasome Activation
Yabal, M., Müller, N., Adler, H., Knies, N., Groß, C. J., Damgaard, R. B., Kanegane, H., Ringelhan, M., Kaufmann, T., Heikenwälder, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.008 · Cited by 255 · see citing works
“The role of XIAP in TNFR signaling has mainly been characterized in mouse embryonic fibroblasts (MEFs).”
HOIP Deficiency Causes Embryonic Lethality by Aberrant TNFR1-Mediated Endothelial Cell Death
Peltzer, N., Rieser, E., Taraborrelli, L., Draber, P., Darding, M., Pernaute, B., Shimizu, Y., Sarr, A., Draberova, H., Montinaro, A., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.066 · Cited by 257 · see citing works
Self-citationMore to Life than NF-κB in TNFR1 Signaling
Ting, A. T., & Bertrand, M. J. M. (2016) · Trends in Immunology · doi:10.1016/j.it.2016.06.002 · Cited by 254 · see citing works
Photoreceptor cell death and rescue in retinal detachment and degenerations
Murakami, Y., Notomi, S., Hisatomi, T., Nakazawa, T., Ishibashi, T., Miller, J. W., & Vavvas, D. G. (2013) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2013.08.001 · Cited by 248 · see citing works
“This cardiac defects in cIap1−/−cIap2−/− mice are rescued by additional Rip1 or Rip3 deficienty (Moulin et al., 2012), suggesting the ubiquitination of RIP1 by cIAPs may negatively regulate RIP kinase activation during development.”
Intracellular regulation of TNF activity in health and disease
Varfolomeev, E. E., & Vucic, D. (2016) · Cytokine · doi:10.1016/j.cyto.2016.08.035 · Cited by 247 · see citing works
Obexer, P., & Ausserlechner, M. J. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00197 · Cited by 245 · see citing works
“Whereas the genetic deletion of XIAP causes only a very mild phenotype in knock-out mice (64, 65), targeting of multiple IAPs, as it is achieved by high affinity SMACmimetics, may be detrimental to an organism as demonstrated by the deletion of cIAP1 together with cIAP2 or XIAP (66).”
BackgroundFigueroa, G., Álvarez-Carrasco, P., Ortega, E., & Maldonado‐Bernal, C. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.631821 · Cited by 218 · see citing works
Roles of RIPK3 in necroptosis, cell signaling, and disease
Morgan, M. J., & Kim, Y. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00868-z · Cited by 189 · see citing works
Holding RIPK1 on the Ubiquitin Leash in TNFR1 Signaling
Peltzer, N., Darding, M., & Walczak, H. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.01.006 · Cited by 184 · see citing works
“[54]”
BackgroundInfluentialPoly-ubiquitination in TNFR1-mediated necroptosis
Dondelinger, Y., Darding, M., Bertrand, M. J. M., & Walczak, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2191-4 · Cited by 173 · see citing works
“Dysregulation of RIPK1 in these knockouts has also been shown genetically since deletion of RIPK1 slightly delays the lethality of cIAP1 cIAP2 animals [63].”
BackgroundRegulation of Apoptosis by Inhibitors of Apoptosis (IAPs)
Berthelet, J., & Dubrez, L. (2013) · Cells · doi:10.3390/cells2010163 · Cited by 177 · see citing works
“Knocking out (KO) of single iap gene in mouse does not lead to obvious developmental abnormalities [86,87], however, a combined deletion of ciap1 with ciap2 or xiap in mice resulted in mid-embryonic lethality due to cardiovascular failure [88].”
BackgroundSNIPERs—Hijacking IAP activity to induce protein degradation
Naito, M., Ohoka, N., & Shibata, N. (2019) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2018.12.002 · Cited by 167 · see citing works
Rodrigue‐Gervais, I. G., Labbè, K., Dagenais, M., Dupaul-Chicoine, J., Champagne, C., Morizot, A., Skeldon, A. M., Brincks, E. L., Vidal, S. M., Griffith, T. S., et al. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2013.12.003 · Cited by 161 · see citing works
Condon, S. M., Mitsuuchi, Y., Deng, Y., LaPorte, M. G., Rippin, S. R., Haimowitz, T., Alexander, M. D., Kumar, P. T., Hendi, M. S., Lee, Y.-H., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500176w · Cited by 153 · see citing works
Self-citationViral modulation of programmed necrosis
Kaiser, W. J., Upton, J. W., & Mocarski, E. S. (2013) · Current Opinion in Virology · doi:10.1016/j.coviro.2013.05.019 · Cited by 149 · see citing works
“Thus, studies that initially centered on RIP1 [69,72] paved the way to discovery of RIP3 [87,117,118] as well as to a conceptual framework where RIP3 in complex with MLKL is now recognized as the central mediator of programmed necrosis [27,89,93,94,119].”
BackgroundSexual Dimorphism of Doxorubicin-Mediated Cardiotoxicity
Moulin, M., Piquereau, J., Matéo, P., Fortin, D., Rücker‐Martin, C., Gressette, M., Lefebvre, F., Grešíková, M., Solgadi, A., Veksler, V., et al. (2014) · Circulation Heart Failure · doi:10.1161/circheartfailure.114.001180 · Cited by 147 · see citing works
Self-citationDisease‐causing mutations in the XIAP BIR2 domain impair NOD2‐dependent immune signalling
Damgaard, R. B., Fiil, B. K., Speckmann, C., Yabal, M., Stadt, U. Z., Bekker‐Jensen, S., Jost, P. J., Ehl, S. R., Mailand, N., & Gyrd‐Hansen, M. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201303090 · Cited by 148 · see citing works
“…pro ‐ in fl ammatory response after TLR2 and TLR4 stimulation, NIK ‐ mediated activation of NF ‐ k B activity and the inhibition of IKK activation downstream of TNF ‐ R1 observed with some SMCs (Bertrand et al, 2008; Moulin et al, 2012; Tseng et al, 2010; Varfolomeev et al, 2007; Vince et al, 2007).”
Ubiquitin-Mediated Regulation of RIPK1 Kinase Activity Independent of IKK and MK2
Annibaldi, A., John, S. W., Berghe, T. V., Swatek, K. N., Ruan, J., Liccardi, G., Bianchi, K., Elliott, P. R., Choi, S. M., Coillie, S. V., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.027 · Cited by 145 · see citing works
“Previous work indicated that cIAP1 and cIAP2 function redundantly to each other (Conte et al., 2006; Conze et al., 2005;Moulin et al., 2012).”
BackgroundMethodSelf-citationXIAP deficiency syndrome in humans
Latour, S., & Aguilar, C. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.01.015 · Cited by 144 · see citing works
Future Therapeutic Directions for Smac-Mimetics
Morrish, E., Brumatti, G., & Silke, J. (2020) · Cells · doi:10.3390/cells9020406 · Cited by 141 · see citing works
“There are two conflicting reports with regard to ciap1−/−/xiap−/− with one strain being embryonic lethal [62] and another viable [63].”
BackgroundInfluentialSelf-citationLinear ubiquitination in immunity
Shimizu, Y., Taraborrelli, L., & Walczak, H. (2015) · Immunological Reviews · doi:10.1111/imr.12309 · Cited by 135 · see citing works
“Intriguingly, cIAP1/ 2-double-deficient mice are rescued by TNFR1 deficiency, at least up until birth (93).”
BackgroundThe roles of FADD in extrinsic apoptosis and necroptosis
Lee, E., Seo, J.-H., Jeong, M.-H., Lee, S.-S., & Song, J.-W. (2012) · BMB Reports · doi:10.5483/bmbrep.2012.45.9.186 · Cited by 137 · see citing works
Lawlor, K. E., Feltham, R., Yabal, M., Conos, S. A., Chen, K. W., Ziehe, S., Graß, C., Zhan, Y., Nguyen, T. A., Hall, C. M., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.073 · Cited by 139 · see citing works
“cIAP1 (Birc2) and cIAP2 (Birc3) mice were generated on a C57BL/6 background (Moulin et al., 2012) and backcrossed to the XIAP-deficient mouse, which had been backcrossed to C57BL/6 mice (n > 10 generations).”
BackgroundMethodInfluentialSelf-citationThe Two Faces of Receptor Interacting Protein Kinase-1
Weinlich, R., & Green, D. R. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.001 · Cited by 127 · see citing works
A Phase I Study of the SMAC-Mimetic Birinapant in Adults with Refractory Solid Tumors or Lymphoma
Amaravadi, R. K., Schilder, R. J., Martin, L. P., Levin, M. J., Graham, M. A., Weng, D. E., & Adjei, A. A. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0475 · Cited by 131 · see citing works
“The sparing of either cIAP2 and/or XIAP likely contributes to the positive tolerability profile of birinapant (30).”
BackgroundAn outline of necrosome triggers
Berghe, T. V., Hassannia, B., & Vandenabeele, P. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2189-y · Cited by 130 · see citing works
IAP Family of Cell Death and Signaling Regulators
Silke, J., & Vucic, D. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801430-1.00002-0 · Cited by 127 · see citing works
Self-citationDiverse ubiquitin linkages regulate RIP kinases-mediated inflammatory and cell death signaling
Witt, A., & Vucic, D. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.33 · Cited by 126 · see citing works
“RIP1-dependent cell death is evident from the rescue of the embryonic lethality of c-IAP1 c-IAP2 /− and c-IAP1 /− XIAP /− mice, as hemizygosity for RIP1 was able to prolong the embryonic survival.(66) The importance of maintaining RIP1”
BackgroundCaspase‐8: not so silently deadly
Feltham, R., Vince, J. E., & Lawlor, K. E. (2017) · Clinical & Translational Immunology · doi:10.1038/cti.2016.83 · Cited by 123 · see citing works
Self-citationOTUB1 modulates c‐IAP1 stability to regulate signalling pathways
Goncharov, T., Niessen, K. S., de Almagro, M. C., Izrael-Tomasevic, A., Fedorova, A. V., Varfolomeev, E. E., Arnott, D. P., Deshayes, K., Kirkpatrick, D. S., & Vucic, D. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.62 · Cited by 118 · see citing works
“However, in the absence of c-IAP proteins, RIP1 and c-IAP ubiquitination cannot occur (Moulin et al , 2012; Varfolomeev et al , 2012).”
TNF and TNF receptors as therapeutic targets for rheumatic diseases and beyond
Siegmund, D., & Wajant, H. (2023) · Nature Reviews Rheumatology · doi:10.1038/s41584-023-01002-7 · Cited by 118 · see citing works
Cellular IAP proteins and LUBAC differentially regulate necrosome-associated RIP1 ubiquitination
de Almagro, M. C., Goncharov, T., Newton, K., & Vucic, D. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.158 · Cited by 114 · see citing works
Multitasking Kinase RIPK1 Regulates Cell Death and InflammationPreprint
Newton, K. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a036368 · Cited by 106 · see citing works
“For example, TNF induces excessive activation of RIPK1 in cells lacking cIAP1 and cIAP2 (Wang et al. 2008; Moulin et al. 2012; Dondelinger et al. 2013; Polykratis et al. 2014), TAK1 (Dondelinger et al.”
BackgroundCell Death and Inflammation – A Vital but Dangerous Liaison
Peltzer, N., & Walczak, H. (2019) · Trends in Immunology · doi:10.1016/j.it.2019.03.006 · Cited by 107 · see citing works
Current translational potential and underlying molecular mechanisms of necroptosis
Molnár, T., Mázló, A., Tslaf, V., Szöllősi, A. G., Emri, G., & Koncz, G. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2094-z · Cited by 107 · see citing works
IAPs, regulators of innate immunity and inflammation
Estornes, Y., & Bertrand, M. J. M. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.03.035 · Cited by 100 · see citing works
“[85] Moulin M, Anderton H, Voss AK, Thomas T, Wong WW, Bankovacki A, et al.”
BackgroundNecroptotic Cell Death Signaling and Execution Pathway: Lessons from Knockout Mice
Belizário, J. E., Cordeiro, L., & Enns, S. C. (2015) · Mediators of Inflammation · doi:10.1155/2015/128076 · Cited by 100 · see citing works
“However, Xiap−/− Clap1−/− and Clap1−/− Clap2−/− double-knockout mice are embryonic lethal and this can be rescued by crossing these animals with Ripk1−/− and Ripk3−/−mice [98].”
Targeting the BIR Domains of Inhibitor of Apoptosis (IAP) Proteins in Cancer Treatment
Cossu, F., Milani, M., Mastrangelo, E., & Lecis, D. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.01.009 · Cited by 99 · see citing works
“embryonic lethal, but XIAP/cIAP2 double knockout mice were viable and fertile [118].”
BackgroundBeyond inflammasomes: emerging function of gasdermins during apoptosis and NETosis
Chen, K. W., Demarco, B., & Brož, P. (2019) · The EMBO Journal · doi:10.15252/embj.2019103397 · Cited by 99 · see citing works
Tang, Y., Tu, H., Zhang, J., Zhao, X., Wang, Y., Qin, J., & Lin, X. (2019) · Nature Communications · doi:10.1038/s41467-019-12033-8 · Cited by 96 · see citing works
Programmed Cell Death in Sepsis Associated Acute Kidney Injury
Wu, Z., Deng, J., Zhou, H., Tan, W., Lin, L., & Yang, J. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.883028 · Cited by 97 · see citing works
Khan, N. R., Lawlor, K. E., Murphy, J. M., & Vince, J. E. (2013) · Current Opinion in Immunology · doi:10.1016/j.coi.2013.10.017 · Cited by 92 · see citing works
Evolution of Our Understanding of XIAP Deficiency
Mudde, A. C. A., Booth, C., & Marsh, R. A. (2021) · Frontiers in Pediatrics · doi:10.3389/fped.2021.660520 · Cited by 89 · see citing works
Chaudhary, A. K., Yadav, N., Bhat, T. A., O’Malley, J., Kumar, S., & Chandra, D. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.07.014 · Cited by 89 · see citing works
“Studies carried out by Vaux and colleagues elegantly demonstrated that mice lacking c-IAP2 and XIAP were viable and fertile whereas mice lacking the combination of c-IAP1 and cIAP2 or c-IAP1 and XIAP died at 10 days post-conception [39].”
BackgroundNecroptosis and neutrophil-associated disorders
Wang, X., Yousefi, S., & Simon, H. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0058-8 · Cited by 89 · see citing works
Necroptosis: A new way of dying?
Hanson, B. (2016) · Cancer Biology & Therapy · doi:10.1080/15384047.2016.1210732 · Cited by 87 · see citing works
“in RIP1 ubiquitination, NF-kB is suppressed and cFLIPs are not produced allowing for Caspase-8 activation.(17,71) To prevent Caspase-8 activation, the long cFLIP isoform (cFLIPL) binds to Procaspase-8, inducing its autocleavage and forming a proteolytic”
BackgroundRecent advances in understanding inhibitor of apoptosis proteins
Lalaoui, N., & Vaux, D. L. (2018) · F1000Research · doi:10.12688/f1000research.16439.1 · Cited by 85 · see citing works
Self-citationXIAP as a multifaceted molecule in Cellular Signaling
Hanifeh, M., & Ataei, F. (2022) · APOPTOSIS · doi:10.1007/s10495-022-01734-z · Cited by 81 · see citing works
Regulation of Innate and Adaptive Antitumor Immunity by IAP Antagonists
Dougan, S. K., & Dougan, M. L. (2018) · Immunotherapy · doi:10.2217/imt-2017-0185 · Cited by 78 · see citing works
True Grit: Programmed Necrosis in Antiviral Host Defense, Inflammation, and Immunogenicity
Mocarski, E. S., Kaiser, W. J., Livingston‐Rosanoff, D., Upton, J. W., & Daley‐Bauer, L. P. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302426 · Cited by 74 · see citing works
“the linear ubiquitination complex results in similar inflammatory outcomes (34, 101, 102), and it was the topic of a recent review (103).”
BackgroundGenetic Regulation of RIPK1 and Necroptosis
Xu, D., Zou, C., & Yuan, J. (2021) · Annual Review of Genetics · doi:10.1146/annurev-genet-071719-022748 · Cited by 76 · see citing works
The role of the IAP E3 ubiquitin ligases in regulating pattern-recognition receptor signalling
Vandenabeele, P., & Bertrand, M. J. M. (2012) · Nature reviews. Immunology · doi:10.1038/nri3325 · Cited by 73 · see citing works
Etemadi, N., Holien, J. K., Chau, D., Dewson, G., Murphy, J. M., Alexander, W. S., Parker, M. W., Silke, J., & Nachbur, U. (2013) · FEBS Journal · doi:10.1111/febs.12419 · Cited by 73 · see citing works
Self-citationUbiquitin Ligases cIAP1 and cIAP2 Limit Cell Death to Prevent Inflammation
Zhang, J., Webster, J. D., Dugger, D. L., Goncharov, T., Roose‐Girma, M., Hung, J., Kwon, Y. C., Vucic, D., Newton, K., & Dixit, V. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.111 · Cited by 67 · see citing works
Necroptosis: A Pathogenic Negotiator in Human Diseases
Chaouhan, H. S., Vinod, C., Mahapatra, N., Yu, S., Wang, I., Chen, K., Yu, T., & Li, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112714 · Cited by 68 · see citing works
“Inhibition of cIAPs or their signaling firmly shifts the pro-survival process into a pro-death process [18].”
BackgroundGrabinger, T., Bode, K. J., Demgenski, J., Seitz, C., Delgado, M. E., Kostadinova, F. I., Reinhold, C., Etemadi, N., Wilhelm, S., Schweinlin, M., et al. (2016) · Gastroenterology · doi:10.1053/j.gastro.2016.11.019 · Cited by 66 · see citing works
“However, combined loss of cIAP1 and cIAP2, or cIAP1 and XIAP results in embryonic lethality.(31) Similarly, intestinal epithelium-specific deletion of RIPK1 does not cause the neonatal lethality observed in the complete RIPK1 knockout, but nevertheless results in massive intestinal inflammation and IEC apoptosis, and…”
BackgroundResultSelf-citationThe role of caspases as executioners of apoptosis
Kumar, S., Dorstyn, L., & Lim, Y. P. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210751 · Cited by 70 · see citing works
Lee, E.-W., Seong, D., Seo, J. H., Jeong, M., Lee, H.-K., & Song, J. J. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2014.234 · Cited by 68 · see citing works
“Most biological studies have focused on cIAP1 rather than cIAP2 because cIAP1 is more highly expressed under normal conditions, suggesting its predominant role.(39) In contrast, the absence of both cIAP1 and cIAP2 is required for complete inhibition of TNFα-mediated survival, suggesting that these inhibitors have redu…”
BackgroundMurphy, J. M., & Silke, J. (2014) · EMBO Reports · doi:10.1002/embr.201337970 · Cited by 66 · see citing works
“Surprisingly, given that TNFR1 is not required for embryonic development, the death of cIAP1/cIAP2 double knock-out mice at E10 can be prevented by simultaneously deleting Tnfr1 [20].”
Self-citationMotawi, T. K., Abdel-Nasser, Z. M., & Shahin, N. N. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00516 · Cited by 62 · see citing works
The Immuno-Modulatory Effects of Inhibitor of Apoptosis Protein Antagonists in Cancer Immunotherapy
Michie, J., Kearney, C. J., Hawkins, E. D., Silke, J., & Oliaro, J. (2020) · Cells · doi:10.3390/cells9010207 · Cited by 64 · see citing works
Self-citationPtpn6 inhibits caspase-8- and Ripk3/Mlkl-dependent inflammation
Speir, M., Nowell, C. J., Chen, A. A., O’Donnell, J. A., Shamie, I., Lakin, P. R., D’Cruz, A. A., Braun, R. O., Babon, J. J., Lewis, R. S., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0550-7 · Cited by 60 · see citing works
IAP-Mediated Protein Ubiquitination in Regulating Cell Signaling
Dumétier, B., Zadoroznyj, A., & Dubrez, L. (2020) · Cells · doi:10.3390/cells9051118 · Cited by 60 · see citing works
Vasilikos, L., Spilgies, L. M., Knop, J., & Wong, W. W.-L. (2016) · Immunology and Cell Biology · doi:10.1038/icb.2016.118 · Cited by 59 · see citing works
Self-citationDED or alive: assembly and regulation of the death effector domain complexes
Riley, J. S., Malik, A., Holohan, C., & Longley, D. B. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.213 · Cited by 57 · see citing works
Controlled detonation: evolution of necroptosis in pathogen defense
Brault, M., & Oberst, A. (2016) · Immunology and Cell Biology · doi:10.1038/icb.2016.117 · Cited by 56 · see citing works
Relevance of necroptosis in cancer
Lalaoui, N., & Brumatti, G. (2016) · Immunology and Cell Biology · doi:10.1038/icb.2016.120 · Cited by 56 · see citing works
IAP proteins: regulators of cell migration and development
Kenneth, N. S., & Duckett, C. S. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.11.004 · Cited by 56 · see citing works
Ju, E., Park, K. A., Shen, H., & Hur, G. M. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00847-4 · Cited by 54 · see citing works
Huang, X., Xiao, F., Li, Y., Qian, W., Ding, W., & Ye, X. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0976-z · Cited by 55 · see citing works
Post-translational control of RIPK3 and MLKL mediated necroptotic cell death
Murphy, J. M., & Vince, J. E. (2015) · F1000Research · doi:10.12688/f1000research.7046.1 · Cited by 53 · see citing works
The interplay of autophagy and non-apoptotic cell death pathways
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.12.004 · Cited by 50 · see citing works
Smac mimetics induce inflammation and necrotic tumour cell death by modulating macrophage activity
Lecis, D., Cesare, M. D., Perego, P., Conti, A., Corna, E., Drago, C., Seneci, P., Walczak, H., Colombo, M. P., Delia, D., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.449 · Cited by 50 · see citing works
Zhao, Q., Yu, X., Zhang, H., Liu, Y., Zhang, X., Wu, X., Xie, Q., Li, M., Ying, H., & Zhang, H. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.011 · Cited by 49 · see citing works
Xu, X., Zhang, T., Xia, X., Yin, Y., Yang, S., Ai, D., Qin, H., Zhou, M., & Song, J. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.953277 · Cited by 49 · see citing works
“In parallel, RIPK3-mediated necroptosis and activation of NLRP3/IL-1b were also enhanced (Tenev et al., 2011; Moulin et al., 2012; Lawlor et al., 2015).”
BackgroundThe roles of ubiquitination in extrinsic cell death pathways and its implications for therapeutics
Seo, J., Kim, M. W., Bae, K., Lee, S. C., Song, J., & Lee, E. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.11.012 · Cited by 47 · see citing works
Collateral damage: necroptosis in the development of lung injury
Faust, H. E., & Mangalmurti, N. S. (2019) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00065.2019 · Cited by 48 · see citing works
- Authors
- Moulin, M., Anderton, H., Voss, A. K., Thomas, T., Wong, W. W., Bankovacki, A., Feltham, R., Chau, D., Cook, W. D., Silke, J., & Vaux, D. L.
- Affiliations
- La Trobe University (AU)
- Walter and Eliza Hall Institute of Medical Research (AU)
- The University of Melbourne (AU)
- Corresponding author
- Vaux, David L
- ORCID
- Venue
- The EMBO Journal
- Published
- 2012-02-10
- Volume
- 31
- Issue
- 7
- Pages
- 1679-1691
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3321198
- OpenAlex
- W1857408336
- Cited by
- 193
- References
- 52
- Citations by year
- 2026: 7 · 2025: 2 · 2024: 2 · 2023: 8 · 2022: 14 · 2021: 17 · 2020: 12 · 2019: 17 · 2018: 12 · 2017: 10 · 2016: 20 · 2015: 23 · 2014: 21 · 2013: 19 · 2012: 9
- FWCI
- 9.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion, other-oa)
- Funders
- Leukemia and Lymphoma Society
- Australian Government
- La Trobe University
- National Health and Medical Research Council (1003435, 461221, 433063, 541901, 575512)
- Japan Society for the Promotion of Science (22689008)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- inhibitor of apoptosis proteins, cIAP1, cIAP2, XIAP, TNF receptor 1, RIPK1, RIPK3, embryonic lethality, cytokine receptor signalling, apoptosis regulation, gene deletion
- MeSH terms
- Animals, Female, Male, Signal Transduction, Gene Deletion, Receptors, Tumor Necrosis Factor, Type I, Receptors, Tumor Necrosis Factor, Type II, Inhibitor of Apoptosis Proteins, Mice, Receptor-Interacting Protein Serine-Threonine Kinases
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