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Volumn 14, Issue 9, 2014, Pages 601-618

A long-awaited merger of the pathways mediating host defence and programmed cell death

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 8; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FLICE INHIBITORY PROTEIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; PATTERN RECOGNITION RECEPTOR; RECEPTOR INTERACTING PROTEIN KINASE 1; RECEPTOR INTERACTING PROTEIN KINASE 3; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG; ABSENT IN MELANOMA 2; CASPASE 11; INFLAMMASOME; INTERLEUKIN 1BETA; LIPOPOLYSACCHARIDE; MITOCHONDRIAL ANTIVIRAL SIGNALLING PROTEIN; RETINOIC ACID INDUCIBLE PROTEIN I; TOLL LIKE RECEPTOR 3; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED DEATH DOMAIN PROTEIN; CARRIER PROTEIN; CASPASE; NLRP3 PROTEIN, HUMAN; RIPK1 PROTEIN, HUMAN; RIPK3 PROTEIN, HUMAN; TICAM1 PROTEIN, HUMAN; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 84906535354     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri3720     Document Type: Review
Times cited : (100)

References (168)
  • 1
    • 84893679891 scopus 로고    scopus 로고
    • Concepts of tissue injury and cell death in inflammation: A historical perspective
    • Wallach, D., Kang, T. B. & Kovalenko, A. Concepts of tissue injury and cell death in inflammation: a historical perspective. Nature Rev. Immunol. 14, 51-59 (2014).
    • (2014) Nature Rev. Immunol , vol.14 , pp. 51-59
    • Wallach, D.1    Kang, T.B.2    Kovalenko, A.3
  • 2
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway, C. A. Jr. Pillars article: approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol. 1989. 54: 1-13. (Pubitemid 20177564)
    • (1989) Cold Spring Harbor Symposia on Quantitative Biology , vol.54 , Issue.1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 3
    • 84885965618 scopus 로고    scopus 로고
    • J. Immunol. 191, 4475-4487 (2013).
    • (2013) J. Immunol , vol.191 , pp. 4475-4487
  • 4
    • 0028201732 scopus 로고
    • Tolerance danger, and the extended family
    • Matzinger, P. Tolerance, danger, and the extended family. Annu. Rev. Immunol. 12, 991-1045 (1994).
    • (1994) Annu. Rev. Immunol , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 5
    • 66949122854 scopus 로고    scopus 로고
    • Approaching the asymptote: 20 years later
    • Medzhitov, R. Approaching the asymptote: 20 years later. Immunity 30, 766-775 (2009).
    • (2009) Immunity , vol.30 , pp. 766-775
    • Medzhitov, R.1
  • 6
    • 66749174867 scopus 로고    scopus 로고
    • The inflammasomes: Guardians of the body
    • Martinon, F., Mayor, A. & Tschopp, J. The inflammasomes: guardians of the body. Annu. Rev. Immunol. 27, 229-265 (2009).
    • (2009) Annu. Rev. Immunol , vol.27 , pp. 229-265
    • Martinon, F.1    Mayor, A.2    Tschopp, J.3
  • 7
    • 0026635783 scopus 로고
    • Shigella flexneri induces apoptosis in infected macrophages
    • Zychlinsky, A., Prevost, M. C. & Sansonetti, P. J. Shigella flexneri induces apoptosis in infected macrophages. Nature 358, 167-169 (1992).
    • (1992) Nature , vol.358 , pp. 167-169
    • Zychlinsky, A.1    Prevost, M.C.2    Sansonetti, P.J.3
  • 8
    • 0028984948 scopus 로고
    • Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock
    • Li, P. et al. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 80, 401-411 (1995).
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1
  • 9
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme
    • Kuida, K. et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 267, 2000-2003 (1995).
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1
  • 11
    • 78650210802 scopus 로고    scopus 로고
    • Differential requirement for caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing
    • Broz, P., von Moltke, J., Jones, J. W., Vance, R. E. & Monack, D. M. Differential requirement for caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing. Cell Host Microbe 8, 471-483 (2010).
    • (2010) Cell Host Microbe , vol.8 , pp. 471-483
    • Broz, P.1    Von Moltke, J.2    Jones, J.W.3    Vance, R.E.4    Monack, D.M.5
  • 12
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • Kayagaki, N. et al. Non-canonical inflammasome activation targets caspase-11. Nature 479, 117-121 (2011).
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1
  • 13
    • 0029005646 scopus 로고
    • A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells
    • Faucheu, C. et al. A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells. EMBO J. 14, 1914-1922 (1995).
    • (1995) EMBO J , vol.14 , pp. 1914-1922
    • Faucheu, C.1
  • 14
    • 0029078965 scopus 로고
    • Identification and characterization of ICH-2, a novel member of the interleukin-1ß-converting enzyme family of cysteine proteases
    • Kamens, J. et al. Identification and characterization of ICH-2, a novel member of the interleukin-1ß-converting enzyme family of cysteine proteases. J. Biol. Chem. 270, 15250-15256 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 15250-15256
    • Kamens, J.1
  • 15
    • 0029032878 scopus 로고
    • Molecular cloning and proapoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases
    • Munday, N. A. et al. Molecular cloning and proapoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases. J. Biol. Chem. 270, 15870-15876 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 15870-15876
    • Munday, N.A.1
  • 16
    • 0029808205 scopus 로고    scopus 로고
    • Identification and characterization of ich-3, a member of the interleukin-1β converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE
    • DOI 10.1074/jbc.271.34.20580
    • Wang, S. et al. Identification and characterization of Ich-3, a member of the interleukin-1ß converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE. J. Biol. Chem. 271, 20580-20587 (1996). (Pubitemid 26281835)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20580-20587
    • Wang, S.1    Miura, M.2    Jung, Y.-K.3    Zhu, H.4    Gagliardini, V.5    Shi, L.6    Greenberg, A.H.7    Yuan, J.8
  • 17
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE
    • DOI 10.1016/S0092-8674(00)80943-5
    • Wang, S. et al. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92, 501-509 (1998). (Pubitemid 28101113)
    • (1998) Cell , vol.92 , Issue.4 , pp. 501-509
    • Wang, S.1    Miura, M.2    Jung, Y.-K.3    Zhu, H.4    Li, E.5    Yuan, J.6
  • 18
    • 0034192466 scopus 로고    scopus 로고
    • Dual role of caspase-11 in mediating activation of caspase-1 and caspase-3 under pathological conditions
    • Kang, S. J. et al. Dual role of caspase-11 in mediating activation of caspase-1 and caspase-3 under pathological conditions. J. Cell Biol. 149, 613-622 (2000).
    • (2000) J. Cell Biol , vol.149 , pp. 613-622
    • Kang, S.J.1
  • 21
    • 77955390094 scopus 로고    scopus 로고
    • Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
    • Broz, P. et al. Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella. J. Exp. Med. 207, 1745-1755 (2010).
    • (2010) J. Exp. Med , vol.207 , pp. 1745-1755
    • Broz, P.1
  • 22
    • 84867333450 scopus 로고    scopus 로고
    • Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1
    • Broz, P. et al. Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1. Nature 490, 288-291 (2012).
    • (2012) Nature , vol.490 , pp. 288-291
    • Broz, P.1
  • 23
    • 84867241369 scopus 로고    scopus 로고
    • Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-ß (TRIF)-mediated caspase-11 protease production integrates Toll-like receptor 4 (TLR4) protein-and Nlrp3 inflammasome-mediated host defense against enteropathogens
    • Gurung, P. et al. Toll or interleukin-1 receptor (TIR) domain-containing adaptor inducing interferon-ß (TRIF)-mediated caspase-11 protease production integrates Toll-like receptor 4 (TLR4) protein-and Nlrp3 inflammasome-mediated host defense against enteropathogens. J. Biol. Chem. 287, 34474-34483 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 34474-34483
    • Gurung, P.1
  • 24
    • 84864600268 scopus 로고    scopus 로고
    • TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gram-negative bacteria
    • Rathinam, V. A. et al. TRIF licenses caspase-11-dependent NLRP3 inflammasome activation by gram-negative bacteria. Cell 150, 606-619 (2012).
    • (2012) Cell , vol.150 , pp. 606-619
    • Rathinam, V.A.1
  • 25
    • 79959242498 scopus 로고    scopus 로고
    • Detection of prokaryotic mRNA signifies microbial viability and promotes immunity
    • Sander, L. E. et al. Detection of prokaryotic mRNA signifies microbial viability and promotes immunity. Nature 474, 385-389 (2011).
    • (2011) Nature , vol.474 , pp. 385-389
    • Sander, L.E.1
  • 26
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O. & Akira, S. Pattern recognition receptors and inflammation. Cell 140, 805-820 (2010).
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 27
    • 84873202976 scopus 로고    scopus 로고
    • Caspase-11 stimulates rapid flagellinindependent pyroptosis in response to Legionella pneumophila
    • Case, C. L. et al. Caspase-11 stimulates rapid flagellinindependent pyroptosis in response to Legionella pneumophila. Proc. Natl Acad. Sci. USA 110, 1851-1856 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 1851-1856
    • Case, C.L.1
  • 28
    • 84879527408 scopus 로고    scopus 로고
    • Caspase-11 activation in response to bacterial secretion systems that access the host cytosol
    • Casson, C. N. et al. Caspase-11 activation in response to bacterial secretion systems that access the host cytosol. PLoS Pathog. 9, e1003400 (2013).
    • (2013) PLoS Pathog , vol.9
    • Casson, C.N.1
  • 29
    • 84874189388 scopus 로고    scopus 로고
    • Caspase-11 protects against bacteria that escape the vacuole
    • Aachoui, Y. et al. Caspase-11 protects against bacteria that escape the vacuole. Science 339, 975-978 (2013).
    • (2013) Science , vol.339 , pp. 975-978
    • Aachoui, Y.1
  • 30
    • 84899953763 scopus 로고    scopus 로고
    • Endosomes are specialized platforms for bacterial sensing and NOD2 signalling
    • Nakamura, N. et al. Endosomes are specialized platforms for bacterial sensing and NOD2 signalling. Nature 509, 240-244 (2014).
    • (2014) Nature , vol.509 , pp. 240-244
    • Nakamura, N.1
  • 31
    • 84900564237 scopus 로고    scopus 로고
    • Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases
    • Meunier, E. et al. Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases. Nature 509, 366-370 (2014).
    • (2014) Nature , vol.509 , pp. 366-370
    • Meunier, E.1
  • 32
    • 84883790050 scopus 로고    scopus 로고
    • Cytoplasmic LPS activates caspase-11: Implications in TLR4-independent endotoxic shock
    • Hagar, J. A., Powell, D. A., Aachoui, Y., Ernst, R. K. & Miao, E. A. Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock. Science 341, 1250-1253 (2013).
    • (2013) Science , vol.341 , pp. 1250-1253
    • Hagar, J.A.1    Powell, D.A.2    Aachoui, Y.3    Ernst, R.K.4    Miao, E.A.5
  • 33
    • 84883775365 scopus 로고    scopus 로고
    • Noncanonical inflammasome activation by intracellular LPS independent of TLR4
    • Kayagaki, N. et al. Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 341, 1246-1249 (2013).
    • (2013) Science , vol.341 , pp. 1246-1249
    • Kayagaki, N.1
  • 34
    • 84897377065 scopus 로고    scopus 로고
    • Why have clinical trials in sepsis failed?
    • Marshall, J. C. Why have clinical trials in sepsis failed? Trends Mol. Med. 20, 195-203 (2014).
    • (2014) Trends Mol. Med , vol.20 , pp. 195-203
    • Marshall, J.C.1
  • 35
    • 84874457770 scopus 로고    scopus 로고
    • Genomic responses in mouse models poorly mimic human inflammatory diseases
    • Seok, J. et al. Genomic responses in mouse models poorly mimic human inflammatory diseases. Proc. Natl Acad. Sci. USA 110, 3507-3512 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 3507-3512
    • Seok, J.1
  • 36
    • 0034704161 scopus 로고    scopus 로고
    • Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-γ
    • DOI 10.1074/jbc.M007255200
    • Lin, X. Y., Choi, M. S. & Porter, A. G. Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-.. J. Biol. Chem. 275, 39920-39926 (2000). (Pubitemid 32064613)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 39920-39926
    • Lin, X.Y.1    Choi, M.S.K.2    Porter, A.G.3
  • 37
    • 84903555072 scopus 로고    scopus 로고
    • A critical role for human caspase-4 in endotoxin sensitivity
    • Kajiwara, Y. et al. A critical role for human caspase-4 in endotoxin sensitivity. J. Immunol. 193, 335-343 (2014).
    • (2014) J. Immunol , vol.193 , pp. 335-343
    • Kajiwara, Y.1
  • 38
    • 84899065546 scopus 로고    scopus 로고
    • The in vivo significance of necroptosis: Lessons from exploration of caspase-8 function
    • Wallach, D., Kang, T. B., Yang, S. H. & Kovalenko, A. The in vivo significance of necroptosis: Lessons from exploration of caspase-8 function. Cytokine Growth Factor Rev. 25, 157-165 (2013).
    • (2013) Cytokine Growth Factor Rev , vol.25 , pp. 157-165
    • Wallach, D.1    Kang, T.B.2    Yang, S.H.3    Kovalenko, A.4
  • 39
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIPL complex inhibits RIPK3-dependent necrosis
    • Oberst, A. et al. Catalytic activity of the caspase-8-FLIPL complex inhibits RIPK3-dependent necrosis. Nature 471, 363-367 (2011).
    • (2011) Nature , vol.471 , pp. 363-367
    • Oberst, A.1
  • 40
    • 80052845560 scopus 로고    scopus 로고
    • Caspase-8 regulates TNF-a-induced epithelial necroptosis and terminal ileitis
    • Gunther, C. et al. Caspase-8 regulates TNF-a-induced epithelial necroptosis and terminal ileitis. Nature 477, 335-339 (2011).
    • (2011) Nature , vol.477 , pp. 335-339
    • Gunther, C.1
  • 42
    • 44849092853 scopus 로고    scopus 로고
    • Cell-autonomous and non-cellautonomous functions of caspase-8
    • Ben Moshe, T. et al. Cell-autonomous and non-cellautonomous functions of caspase-8. Cytokine Growth Factor Rev. 19, 209-217 (2008).
    • (2008) Cytokine Growth Factor Rev , vol.19 , pp. 209-217
    • Ben Moshe, T.1
  • 43
    • 70350484946 scopus 로고    scopus 로고
    • Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease
    • Kovalenko, A. et al. Caspase-8 deficiency in epidermal keratinocytes triggers an inflammatory skin disease. J. Exp. Med. 206, 2161-2177 (2009).
    • (2009) J. Exp. Med , vol.206 , pp. 2161-2177
    • Kovalenko, A.1
  • 44
    • 79952811804 scopus 로고    scopus 로고
    • RIP3 mediates the embryonic lethality of caspase-8-deficient mice
    • Kaiser, W. J. et al. RIP3 mediates the embryonic lethality of caspase-8-deficient mice. Nature 471, 368-372 (2011).
    • (2011) Nature , vol.471 , pp. 368-372
    • Kaiser, W.J.1
  • 46
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • DOI 10.1016/j.cellsig.2007.05.016, PII S089865680700157X
    • Feng, S. et al. Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell Signal 19, 2056-2067 (2007). (Pubitemid 47353808)
    • (2007) Cellular Signalling , vol.19 , Issue.10 , pp. 2056-2067
    • Feng, S.1    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.-e.5    Hoti, N.6    Castanares, M.7    Wu, M.8
  • 47
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by Caspase-8 prompts TNF-induced apoptosis
    • DOI 10.1101/gad.13.19.2514
    • Lin, Y., Devin, A., Rodriguez, Y. & Liu, Z. G. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev. 13, 2514-2526 (1999). (Pubitemid 29489643)
    • (1999) Genes and Development , vol.13 , Issue.19 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.-G.4
  • 48
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho, Y. S. et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137, 1112-1123 (2009).
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1
  • 49
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-a
    • He, S. et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-a. Cell 137, 1100-1111 (2009).
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 50
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang, D. W. et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 325, 332-336 (2009).
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1
  • 52
    • 17144413785 scopus 로고    scopus 로고
    • Apoptosis induced by the toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif
    • Kaiser, W. J. & Offermann, M. K. Apoptosis induced by the toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif. J. Immunol. 174, 4942-4952 (2005). (Pubitemid 40514460)
    • (2005) Journal of Immunology , vol.174 , Issue.8 , pp. 4942-4952
    • Kaiser, W.J.1    Offermann, M.K.2
  • 53
    • 2442605662 scopus 로고    scopus 로고
    • Mechanisms of the TRIF-induced interferon-stimulated response element and NF-.B activation and apoptosis pathways
    • Han, K. J. et al. Mechanisms of the TRIF-induced interferon-stimulated response element and NF-.B activation and apoptosis pathways. J. Biol. Chem. 279, 15652-15661 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 15652-15661
    • Han, K.J.1
  • 54
    • 0141923690 scopus 로고    scopus 로고
    • Toll/IL-1 receptor domain-containing adaptor inducing IFN-β (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-κB and IFN-regulatory factor-3, in the toll-like receptor signaling
    • Sato, S. et al. Toll/IL-1 receptor domain-containing adaptor inducing IFN-ß (TRIF) associates with TNF receptor-associated factor 6 and TANK-binding kinase 1, and activates two distinct transcription factors, NF-. B and IFN-regulatory factor-3, in the Toll-like receptor signaling. J. Immunol. 171, 4304-4310 (2003). (Pubitemid 37238709)
    • (2003) Journal of Immunology , vol.171 , Issue.8 , pp. 4304-4310
    • Sato, S.1    Sugiyama, M.2    Yamamoto, M.3    Watanabe, Y.4    Kawai, T.5    Takeda, K.6    Akira, S.7
  • 55
    • 27744561393 scopus 로고    scopus 로고
    • Rip1 mediates the trif-dependent Toll-like receptor 3- and 4-induced NF-κB activation but does not contribute to interferon regulatory factor 3 activation
    • DOI 10.1074/jbc.M506831200
    • Cusson-Hermance, N., Khurana, S., Lee, T. H., Fitzgerald, K. A. & Kelliher, M. A. Rip1 mediates the Trif-dependent toll-like receptor 3-and 4-induced NF-.B activation but does not contribute to interferon regulatory factor 3 activation. J. Biol. Chem. 280, 36560-36566 (2005). (Pubitemid 41587731)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.44 , pp. 36560-36566
    • Cusson-Hermance, N.1    Khurana, S.2    Lee, T.H.3    Fitzgerald, K.A.4    Kelliher, M.A.5
  • 56
    • 50049125047 scopus 로고    scopus 로고
    • Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIFdependent inflammatory responses
    • Ermolaeva, M. A. et al. Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIFdependent inflammatory responses. Nature Immunol. 9, 1037-1046 (2008).
    • (2008) Nature Immunol , vol.9 , pp. 1037-1046
    • Ermolaeva, M.A.1
  • 57
    • 84055181328 scopus 로고    scopus 로고
    • Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3-mediated pathway
    • He, S., Liang, Y., Shao, F. & Wang, X. Toll-like receptors activate programmed necrosis in macrophages through a receptor-interacting kinase-3-mediated pathway. Proc. Natl Acad. Sci. USA 108, 20054-20059 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 20054-20059
    • He, S.1    Liang, Y.2    Shao, F.3    Wang, X.4
  • 58
    • 84886656964 scopus 로고    scopus 로고
    • Toll-like receptor 3-mediated necrosis via TRIF RIP3, and MLKL
    • Kaiser, W. J. et al. Toll-like receptor 3-mediated necrosis via TRIF, RIP3, and MLKL. J. Biol. Chem. 288, 31268-31279 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 31268-31279
    • Kaiser, W.J.1
  • 60
    • 29644433629 scopus 로고    scopus 로고
    • NF-κB protects macrophages from lipopolysaccharide-induced cell death: The role of caspase 8 and receptor-interacting protein
    • DOI 10.1074/jbc.M510849200
    • Ma, Y., Temkin, V., Liu, H. & Pope, R. M. NF-.B protects macrophages from lipopolysaccharideinduced cell death: the role of caspase 8 and receptor-interacting protein. J. Biol. Chem. 280, 41827-41834 (2005). (Pubitemid 43023151)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.51 , pp. 41827-41834
    • Ma, Y.1    Temkin, V.2    Liu, H.3    Pope, R.M.4
  • 61
    • 79960922705 scopus 로고    scopus 로고
    • CIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • Feoktistova, M. et al. cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol. Cell 43, 449-463 (2011).
    • (2011) Mol. Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1
  • 62
    • 79960921946 scopus 로고    scopus 로고
    • The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • Tenev, T. et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol. Cell 43, 432-448 (2011).
    • (2011) Mol. Cell , vol.43 , pp. 432-448
    • Tenev, T.1
  • 64
    • 84901386193 scopus 로고    scopus 로고
    • RIPK1 blocks early postnatal lethality mediated by caspase-8 and RIPK3
    • Dillon, C. P. et al. RIPK1 blocks early postnatal lethality mediated by caspase-8 and RIPK3. Cell 157, 1189-1202 (2014).
    • (2014) Cell , vol.157 , pp. 1189-1202
    • Dillon, C.P.1
  • 65
    • 84901649808 scopus 로고    scopus 로고
    • RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition
    • Kaiser, W. J. et al. RIP1 suppresses innate immune necrotic as well as apoptotic cell death during mammalian parturition. Proc. Natl Acad. Sci. USA 111, 7753-7758 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 7753-7758
    • Kaiser, W.J.1
  • 66
    • 84901422731 scopus 로고    scopus 로고
    • RIPK1 regulates RIPK3-MLKLdriven systemic inflammation and emergency hematopoiesis
    • Rickard, J. A. et al. RIPK1 regulates RIPK3-MLKLdriven systemic inflammation and emergency hematopoiesis. Cell 157, 1175-1188 (2014).
    • (2014) Cell , vol.157 , pp. 1175-1188
    • Rickard, J.A.1
  • 67
    • 84897088275 scopus 로고    scopus 로고
    • Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis
    • Newton, K. et al. Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis. Science 343, 1357-1360 (2014).
    • (2014) Science , vol.343 , pp. 1357-1360
    • Newton, K.1
  • 68
    • 84901678314 scopus 로고    scopus 로고
    • Cutting Edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice
    • Berger, S. B. et al. Cutting Edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice. J. Immunol. 192, 5476-5480 (2014).
    • (2014) J. Immunol , vol.192 , pp. 5476-5480
    • Berger, S.B.1
  • 69
    • 84905970879 scopus 로고    scopus 로고
    • Cutting Edge: RIPK1 kinase inactive mice are viable and protected from TNF-induced necroptosis in vivo
    • Polykratis, A. et al. Cutting Edge: RIPK1 kinase inactive mice are viable and protected from TNF-induced necroptosis in vivo. J. Immunol. http://dx.doi.org/10.4049/jimmunol.1400590 (2014).
    • (2014) J. Immunol.
    • Polykratis, A.1
  • 70
    • 84881027178 scopus 로고    scopus 로고
    • Cell death programs in Yersinia immunity and pathogenesis
    • Philip, N. H. & Brodsky, I. E. Cell death programs in Yersinia immunity and pathogenesis. Front. Cell. Infect. Microbiol. 2, 149 (2012).
    • (2012) Front. Cell. Infect. Microbiol , vol.2 , pp. 149
    • Philip, N.H.1    Brodsky, I.E.2
  • 71
    • 84901020402 scopus 로고    scopus 로고
    • Caspase-8 mediates caspase-1 processing and innate immune defense in response to bacterial blockade of NF-κB and MAPK signaling
    • Philip, N. H. et al. Caspase-8 mediates caspase-1 processing and innate immune defense in response to bacterial blockade of NF-κB and MAPK signaling. Proc. Natl Acad. Sci. USA http://dx.doi.org/10.1073/pnas.1403252111 (2014).
    • (2014) Proc. Natl Acad. Sci. USA
    • Philip, N.H.1
  • 72
    • 84901045151 scopus 로고    scopus 로고
    • Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death
    • Weng, D. et al. Caspase-8 and RIP kinases regulate bacteria-induced innate immune responses and cell death. Proc. Natl Acad. Sci. USA http://dx.doi.org/10.1073/pnas.1403477111 (2014).
    • (2014) Proc. Natl Acad. Sci. USA
    • Weng, D.1
  • 75
    • 58149149839 scopus 로고    scopus 로고
    • TLR3 is an endogenous sensor of tissue necrosis during acute inflammatory events
    • Cavassani, K. A. et al. TLR3 is an endogenous sensor of tissue necrosis during acute inflammatory events. J. Exp. Med. 205, 2609-2621 (2008).
    • (2008) J. Exp. Med , vol.205 , pp. 2609-2621
    • Cavassani, K.A.1
  • 77
    • 84875981860 scopus 로고    scopus 로고
    • MAVS-mediated apoptosis and its inhibition by viral proteins
    • Lei, Y. et al. MAVS-mediated apoptosis and its inhibition by viral proteins. PloS ONE 4, e5466 (2009).
    • (2009) PloS ONE , vol.4
    • Lei, Y.1
  • 78
    • 77649202152 scopus 로고    scopus 로고
    • The interferon stimulator mitochondrial antiviral signaling protein facilitates cell death by disrupting the mitochondrial membrane potential and by activating caspases
    • Yu, C. Y., Chiang, R. L., Chang, T. H., Liao, C. L. & Lin, Y. L. The interferon stimulator mitochondrial antiviral signaling protein facilitates cell death by disrupting the mitochondrial membrane potential and by activating caspases. J. Virol. 84, 2421-2431 (2010).
    • (2010) J. Virol , vol.84 , pp. 2421-2431
    • Yu, C.Y.1    Chiang, R.L.2    Chang, T.H.3    Liao, C.L.4    Lin, Y.L.5
  • 79
    • 84894177433 scopus 로고    scopus 로고
    • A bicistronic MAVS transcript highlights a class of truncated variants in antiviral immunity
    • Brubaker, S. W., Gauthier, A. E., Mills, E. W., Ingolia, N. T. & Kagan, J. C. A bicistronic MAVS transcript highlights a class of truncated variants in antiviral immunity. Cell 156, 800-811 (2014).
    • (2014) Cell , vol.156 , pp. 800-811
    • Brubaker, S.W.1    Gauthier, A.E.2    Mills, E.W.3    Ingolia, N.T.4    Kagan, J.C.5
  • 80
    • 9244236078 scopus 로고    scopus 로고
    • A FADD-dependent innate immune mechanism in mammalian cells
    • DOI 10.1038/nature03124
    • Balachandran, S., Thomas, E. & Barber, G. N. A FADD-dependent innate immune mechanism in mammalian cells. Nature 432, 401-405 (2004). (Pubitemid 39551675)
    • (2004) Nature , vol.432 , Issue.7015 , pp. 401-405
    • Balachandran, S.1    Thomas, E.2    Barber, G.N.3
  • 82
    • 43049174990 scopus 로고    scopus 로고
    • TRADD protein is an essential component of the RIG-like helicase antiviral pathway
    • Michallet, M. C. et al. TRADD protein is an essential component of the RIG-like helicase antiviral pathway. Immunity 28, 651-661 (2008).
    • (2008) Immunity , vol.28 , pp. 651-661
    • Michallet, M.C.1
  • 83
    • 33645786318 scopus 로고    scopus 로고
    • Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA
    • Takahashi, K. et al. Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA. J. Immunol. 176, 4520-4524 (2006).
    • (2006) J. Immunol , vol.176 , pp. 4520-4524
    • Takahashi, K.1
  • 84
    • 79952770123 scopus 로고    scopus 로고
    • RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein
    • Rajput, A. et al. RIG-I RNA helicase activation of IRF3 transcription factor is negatively regulated by caspase-8-mediated cleavage of the RIP1 protein. Immunity 34, 340-351 (2011).
    • (2011) Immunity , vol.34 , pp. 340-351
    • Rajput, A.1
  • 85
    • 80052989433 scopus 로고    scopus 로고
    • Caspase-8-mediated cleavage inhibits IRF-3 protein by facilitating its proteasome-mediated degradation
    • Sears, N., Sen, G. C., Stark, G. R. & Chattopadhyay, S. Caspase-8-mediated cleavage inhibits IRF-3 protein by facilitating its proteasome-mediated degradation. J. Biol. Chem. 286, 33037-33044 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 33037-33044
    • Sears, N.1    Sen, G.C.2    Stark, G.R.3    Chattopadhyay, S.4
  • 86
    • 33344476184 scopus 로고    scopus 로고
    • CFLIP regulation of lymphocyte activation and development
    • DOI 10.1038/nri1787
    • Budd, R. C., Yeh, W. C. & Tschopp, J. cFLIP regulation of lymphocyte activation and development. Nature Rev. Immunol. 6, 196-204 (2006). (Pubitemid 43290989)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.3 , pp. 196-204
    • Budd, R.C.1    Yeh, W.-C.2    Tschopp, J.3
  • 87
    • 14644406398 scopus 로고    scopus 로고
    • The flip side of FLIP
    • Peter, M. E. The flip side of FLIP. Biochem. J. 382, e1-e3 (2004).
    • (2004) Biochem. J , vol.382
    • Peter, M.E.1
  • 88
    • 84899131835 scopus 로고    scopus 로고
    • The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling
    • Cai, X., Chiu, Y. H. & Chen, Z. J. The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling. Mol. Cell 54, 289-296 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 289-296
    • Cai, X.1    Chiu, Y.H.2    Chen, Z.J.3
  • 89
    • 84878190840 scopus 로고    scopus 로고
    • Immune sensing of DNA
    • Paludan, S. R. & Bowie, A. G. Immune sensing of DNA. Immunity 38, 870-880 (2013).
    • (2013) Immunity , vol.38 , pp. 870-880
    • Paludan, S.R.1    Bowie, A.G.2
  • 90
    • 84884138508 scopus 로고    scopus 로고
    • The interferon response to intracellular DNA: Why so many receptors?
    • Unterholzner, L. The interferon response to intracellular DNA: why so many receptors? Immunobiology 218, 1312-1321 (2013).
    • (2013) Immunobiology , vol.218 , pp. 1312-1321
    • Unterholzner, L.1
  • 91
    • 77951263260 scopus 로고    scopus 로고
    • The AIM2 inflammasome is critical for innate immunity to Francisella tularensis
    • Fernandes-Alnemri, T. et al. The AIM2 inflammasome is critical for innate immunity to Francisella tularensis. Nature Immunol. 11, 385-393 (2010).
    • (2010) Nature Immunol , vol.11 , pp. 385-393
    • Fernandes-Alnemri, T.1
  • 92
    • 77953116282 scopus 로고    scopus 로고
    • Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis
    • Jones, J. W. et al. Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis. Proc. Natl Acad. Sci. USA 107, 9771-9776 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9771-9776
    • Jones, J.W.1
  • 93
    • 84866087868 scopus 로고    scopus 로고
    • AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages
    • Pierini, R. et al. AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages. Cell Death Differ. 19, 1709-1721 (2012).
    • (2012) Cell Death Differ , vol.19 , pp. 1709-1721
    • Pierini, R.1
  • 94
    • 84882280029 scopus 로고    scopus 로고
    • AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC
    • Sagulenko, V. et al. AIM2 and NLRP3 inflammasomes activate both apoptotic and pyroptotic death pathways via ASC. Cell Death Differ. 20, 1149-1160 (2013).
    • (2013) Cell Death Differ , vol.20 , pp. 1149-1160
    • Sagulenko, V.1
  • 96
    • 58749100879 scopus 로고    scopus 로고
    • Receptor-interacting protein homotypic interaction motif-dependent control of NF-κB activation via the DNA-dependent activator of IFN regulatory factors
    • Kaiser, W. J., Upton, J. W. & Mocarski, E. S. Receptor-interacting protein homotypic interaction motif-dependent control of NF-κB activation via the DNA-dependent activator of IFN regulatory factors. J. Immunol. 181, 6427-6434 (2008).
    • (2008) J. Immunol , vol.181 , pp. 6427-6434
    • Kaiser, W.J.1    Upton, J.W.2    Mocarski, E.S.3
  • 97
    • 68249113997 scopus 로고    scopus 로고
    • DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-κB
    • Rebsamen, M. et al. DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-κB. EMBO Rep. 10, 916-922 (2009).
    • (2009) EMBO Rep , vol.10 , pp. 916-922
    • Rebsamen, M.1
  • 99
    • 84858420051 scopus 로고    scopus 로고
    • DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA
    • Upton, J. W., Kaiser, W. J. & Mocarski, E. S. DAI/ZBP1/DLM-1 complexes with RIP3 to mediate virus-induced programmed necrosis that is targeted by murine cytomegalovirus vIRA. Cell Host Microbe 11, 290-297 (2012).
    • (2012) Cell Host Microbe , vol.11 , pp. 290-297
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 100
    • 33947717153 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by interaction with NALP1
    • Bruey, J. M. et al. Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by interaction with NALP1. Cell 129, 45-56 (2007).
    • (2007) Cell , vol.129 , pp. 45-56
    • Bruey, J.M.1
  • 101
    • 84862777872 scopus 로고    scopus 로고
    • Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
    • Shimada, K. et al. Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity 36, 401-414 (2012).
    • (2012) Immunity , vol.36 , pp. 401-414
    • Shimada, K.1
  • 102
    • 84857404572 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation
    • Vince, J. E. et al. Inhibitor of apoptosis proteins limit RIP3 kinase-dependent interleukin-1 activation. Immunity 36, 215-227 (2012).
    • (2012) Immunity , vol.36 , pp. 215-227
    • Vince, J.E.1
  • 103
    • 84872764927 scopus 로고    scopus 로고
    • Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome
    • Kang, T. B., Yang, S. H., Toth, B., Kovalenko, A. & Wallach, D. Caspase-8 blocks kinase RIPK3-mediated activation of the NLRP3 inflammasome. Immunity 38, 27-40 (2013).
    • (2013) Immunity , vol.38 , pp. 27-40
    • Kang, T.B.1    Yang, S.H.2    Toth, B.3    Kovalenko, A.4    Wallach, D.5
  • 104
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • Sun, L. et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 148, 213-227 (2012).
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1
  • 105
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang, Z., Jiang, H., Chen, S., Du, F. & Wang, X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 148, 228-243 (2012).
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.1    Jiang, H.2    Chen, S.3    Du, F.4    Wang, X.5
  • 106
    • 84859467770 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
    • Zhao, J. et al. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc. Natl Acad. Sci. USA 109, 5322-5327 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 5322-5327
    • Zhao, J.1
  • 107
    • 84884308522 scopus 로고    scopus 로고
    • The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism
    • Murphy, J. M. et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 39, 443-453 (2013).
    • (2013) Immunity , vol.39 , pp. 443-453
    • Murphy, J.M.1
  • 108
    • 84901257054 scopus 로고    scopus 로고
    • Depletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis
    • Remijsen, Q. et al. Depletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis. Cell Death Dis. 5, e1004 (2014).
    • (2014) Cell Death Dis , vol.5
    • Remijsen, Q.1
  • 109
    • 84888438277 scopus 로고    scopus 로고
    • Widespread mitochondrial depletion via mitophagy does not compromise necroptosis
    • Tait, S. W. et al. Widespread mitochondrial depletion via mitophagy does not compromise necroptosis. Cell Rep. 5, 878-885 (2013).
    • (2013) Cell Rep , vol.5 , pp. 878-885
    • Tait, S.W.1
  • 110
    • 84891739370 scopus 로고    scopus 로고
    • Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death
    • Chen, X. et al. Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death. Cell Res. 24, 105-121 (2014).
    • (2014) Cell Res , vol.24 , pp. 105-121
    • Chen, X.1
  • 111
    • 84883770753 scopus 로고    scopus 로고
    • RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition
    • Dondelinger, Y. et al. RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition. Cell Death Differ. 20, 1381-1392 (2013).
    • (2013) Cell Death Differ , vol.20 , pp. 1381-1392
    • Dondelinger, Y.1
  • 112
    • 84898027331 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3
    • Wang, H. et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol. Cell 54, 133-146 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 133-146
    • Wang, H.1
  • 113
    • 84891343566 scopus 로고    scopus 로고
    • Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
    • Cai, Z. et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nature Cell Biol. 16, 55-65 (2014).
    • (2014) Nature Cell Biol , vol.16 , pp. 55-65
    • Cai, Z.1
  • 114
    • 0842304221 scopus 로고    scopus 로고
    • Kinase RIP3 Is Dispensable for Normal NF-κBs, Signaling by the B-Cell and T-Cell Receptors, Tumor Necrosis Factor Receptor 1, and Toll-Like Receptors 2 and 4
    • DOI 10.1128/MCB.24.4.1464-1469.2004
    • Newton, K., Sun, X. & Dixit, V. M. Kinase RIP3 is dispensable for normal NF-κBs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4. Mol. Cell. Biol. 24, 1464-1469 (2004). (Pubitemid 38167070)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.4 , pp. 1464-1469
    • Newton, K.1    Sun, X.2    Dixit, V.M.3
  • 115
    • 70249138036 scopus 로고    scopus 로고
    • Cutting edge: NF-κB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression
    • Bauernfeind, F. G. et al. Cutting edge: NF-κB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J. Immunol. 183, 787-791 (2009).
    • (2009) J. Immunol , vol.183 , pp. 787-791
    • Bauernfeind, F.G.1
  • 116
    • 84896500701 scopus 로고    scopus 로고
    • Cutting Edge: Endoplasmic reticulum stress licenses macrophages to produce mature IL-1β in response to TLR4 stimulation through a caspase-8-and TRIF-dependent pathway
    • Shenderov, K. et al. Cutting Edge: Endoplasmic reticulum stress licenses macrophages to produce mature IL-1β in response to TLR4 stimulation through a caspase-8-and TRIF-dependent pathway. J. Immunol. 192, 2029-2033 (2014).
    • (2014) J. Immunol , vol.192 , pp. 2029-2033
    • Shenderov, K.1
  • 117
    • 84871125002 scopus 로고    scopus 로고
    • Cutting edge: FAS (CD95) mediates noncanonical IL-1β and IL-18 maturation via caspase-8 in an RIP3-independent manner
    • Bossaller, L. et al. Cutting edge: FAS (CD95) mediates noncanonical IL-1β and IL-18 maturation via caspase-8 in an RIP3-independent manner. J. Immunol. 189, 5508-5512 (2012).
    • (2012) J. Immunol , vol.189 , pp. 5508-5512
    • Bossaller, L.1
  • 118
    • 84857175933 scopus 로고    scopus 로고
    • Dectin-1 is an extracellular pathogen sensor for the induction and processing of IL-1β via a noncanonical caspase-8 inflammasome
    • Gringhuis, S. I. et al. Dectin-1 is an extracellular pathogen sensor for the induction and processing of IL-1β via a noncanonical caspase-8 inflammasome. Nature Immunol. 13, 246-254 (2012).
    • (2012) Nature Immunol , vol.13 , pp. 246-254
    • Gringhuis, S.I.1
  • 119
    • 51049100571 scopus 로고    scopus 로고
    • Stimulation of Toll-like receptor 3 and 4 induces interleukin-1β maturation by caspase-8
    • Maelfait, J. et al. Stimulation of Toll-like receptor 3 and 4 induces interleukin-1β maturation by caspase-8. J. Exp. Med. 205, 1967-1973 (2008).
    • (2008) J. Exp. Med , vol.205 , pp. 1967-1973
    • Maelfait, J.1
  • 120
    • 84894271641 scopus 로고    scopus 로고
    • FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes
    • Gurung, P. et al. FADD and caspase-8 mediate priming and activation of the canonical and noncanonical Nlrp3 inflammasomes. J. Immunol. 192, 1835-1846 (2014).
    • (2014) J. Immunol , vol.192 , pp. 1835-1846
    • Gurung, P.1
  • 121
    • 84887439544 scopus 로고    scopus 로고
    • Salmonella infection induces recruitment of caspase-8 to the inflammasome to modulate IL-1β production
    • Man, S. M. et al. Salmonella infection induces recruitment of caspase-8 to the inflammasome to modulate IL-1β production. J. Immunol. 191, 5239-5246 (2013).
    • (2013) J. Immunol , vol.191 , pp. 5239-5246
    • Man, S.M.1
  • 122
    • 84856857478 scopus 로고    scopus 로고
    • ER stress activates the NLRP3 inflammasome via an UPR-independent pathway
    • Menu, P. et al. ER stress activates the NLRP3 inflammasome via an UPR-independent pathway. Cell Death Dis. 3, e261 (2012).
    • (2012) Cell Death Dis , vol.3
    • Menu, P.1
  • 123
    • 79953066407 scopus 로고    scopus 로고
    • HMGB1 is a therapeutic target for sterile inflammation and infection
    • Andersson, U. & Tracey, K. J. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu. Rev. Immunol. 29, 139-162 (2011).
    • (2011) Annu. Rev. Immunol , vol.29 , pp. 139-162
    • Andersson, U.1    Tracey, K.J.2
  • 124
    • 84893850623 scopus 로고    scopus 로고
    • Participation of c-FLIP in NLRP3 and AIM2 inflammasome activation
    • Wu, Y. H. et al. Participation of c-FLIP in NLRP3 and AIM2 inflammasome activation. Cell Death Differ. 21, 451-461 (2014).
    • (2014) Cell Death Differ , vol.21 , pp. 451-461
    • Wu, Y.H.1
  • 125
    • 80054888589 scopus 로고    scopus 로고
    • It cuts both ways: Reconciling the dual roles of caspase 8 in cell death and survival
    • Oberst, A. & Green, D. R. It cuts both ways: reconciling the dual roles of caspase 8 in cell death and survival. Nature Rev. Mol. Cell Biol. 12, 757-763 (2011).
    • (2011) Nature Rev. Mol. Cell Biol , vol.12 , pp. 757-763
    • Oberst, A.1    Green, D.R.2
  • 126
    • 84872469150 scopus 로고    scopus 로고
    • Nineteenth century research on cell death
    • Clarke, P. G. & Clarke, S. Nineteenth century research on cell death. Exp. Oncol. 34, 139-145 (2012).
    • (2012) Exp. Oncol , vol.34 , pp. 139-145
    • Clarke, P.G.1    Clarke, S.2
  • 127
    • 84255210700 scopus 로고    scopus 로고
    • Molecular definitions of cell death subroutines: Recommendations of the Nomenclature Committee on Cell Death 2012
    • Galluzzi, L. et al. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ. 19, 107-120 (2012).
    • (2012) Cell Death Differ , vol.19 , pp. 107-120
    • Galluzzi, L.1
  • 128
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait, S. W. & Green, D. R. Mitochondria and cell death: outer membrane permeabilization and beyond. Nature Rev. Mol. Cell Biol. 11, 621-632 (2010).
    • (2010) Nature Rev. Mol. Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 130
    • 0033815330 scopus 로고    scopus 로고
    • Salmonella induces macrophage death by caspase-1-dependent necrosis
    • Brennan, M. A. & Cookson, B. T. Salmonella induces macrophage death by caspase-1-dependent necrosis. Mol. Microbiol. 38, 31-40 (2000).
    • (2000) Mol. Microbiol , vol.38 , pp. 31-40
    • Brennan, M.A.1    Cookson, B.T.2
  • 131
    • 84881542521 scopus 로고    scopus 로고
    • Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection
    • Aachoui, Y., Sagulenko, V., Miao, E. A. & Stacey, K. J. Inflammasome-mediated pyroptotic and apoptotic cell death, and defense against infection. Curr. Opin. Microbiol. 16, 319-326 (2013).
    • (2013) Curr. Opin. Microbiol , vol.16 , pp. 319-326
    • Aachoui, Y.1    Sagulenko, V.2    Miao, E.A.3    Stacey, K.J.4
  • 133
    • 84906534459 scopus 로고    scopus 로고
    • Snap Shot: Necroptosis
    • Zhou, W. & Yuan, J. SnapShot: Necroptosis. Cell 158, 464-464.e1 (2014).
    • (2014) Cell , vol.158
    • Zhou, W.1    Yuan, J.2
  • 134
    • 84864240409 scopus 로고    scopus 로고
    • The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
    • Li, J. et al. The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150, 339-350 (2012).
    • (2012) Cell , vol.150 , pp. 339-350
    • Li, J.1
  • 136
    • 84874263775 scopus 로고    scopus 로고
    • Necroptosis: The release of damage-associated molecular patterns and its physiological relevance
    • Kaczmarek, A., Vandenabeele, P. & Krysko, D. V. Necroptosis: the release of damage-associated molecular patterns and its physiological relevance. Immunity 38, 209-223 (2013).
    • (2013) Immunity , vol.38 , pp. 209-223
    • Kaczmarek, A.1    Vandenabeele, P.2    Krysko, D.V.3
  • 137
    • 84896690342 scopus 로고    scopus 로고
    • Apoptotic cell clearance: Basic biology and therapeutic potential
    • Poon, I. K., Lucas, C. D., Rossi, A. G. & Ravichandran, K. S. Apoptotic cell clearance: basic biology and therapeutic potential. Nature Rev. Immunol. 14, 166-180 (2014).
    • (2014) Nature Rev. Immunol , vol.14 , pp. 166-180
    • Poon, I.K.1    Lucas, C.D.2    Rossi, A.G.3    Ravichandran, K.S.4
  • 138
    • 79953687375 scopus 로고    scopus 로고
    • The unexpected link between infection-induced apoptosis and a TH17 immune response
    • Brereton, C. F. & Blander, J. M. The unexpected link between infection-induced apoptosis and a TH17 immune response. J. Leukoc. Biol. 89, 565-576 (2011).
    • (2011) J. Leukoc. Biol , vol.89 , pp. 565-576
    • Brereton, C.F.1    Blander, J.M.2
  • 139
    • 84903168901 scopus 로고    scopus 로고
    • Death-defining immune responses after apoptosis
    • Campisi, L., Cummings, R. J. & Blander, J. M. Death-defining immune responses after apoptosis. Am. J. Transplant 14, 1488-1498 (2014).
    • (2014) Am. J. Transplant , vol.14 , pp. 1488-1498
    • Campisi, L.1    Cummings, R.J.2    Blander, J.M.3
  • 140
    • 61949472508 scopus 로고    scopus 로고
    • Innate immune recognition of infected apoptotic cells directs TH17 cell differentiation
    • Torchinsky, M. B., Garaude, J., Martin, A. P. & Blander, J. M. Innate immune recognition of infected apoptotic cells directs TH17 cell differentiation. Nature 458, 78-82 (2009).
    • (2009) Nature , vol.458 , pp. 78-82
    • Torchinsky, M.B.1    Garaude, J.2    Martin, A.P.3    Blander, J.M.4
  • 145
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Yeh, W. C. et al. FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science 279, 1954-1958 (1998).
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1
  • 146
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activationinduced T-cell proliferation are defective in mice lacking FADD/Mort1
    • Zhang, J., Cado, D., Chen, A., Kabra, N. H. & Winoto, A. Fas-mediated apoptosis and activationinduced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 392, 296-300 (1998).
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 147
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • Yeh, W. C. et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity 12, 633-642 (2000).
    • (2000) Immunity , vol.12 , pp. 633-642
    • Yeh, W.C.1
  • 148
    • 84861712290 scopus 로고    scopus 로고
    • Survival function of the FADD-CASPASE-8-cFLIPL complex
    • Dillon, C. P. et al. Survival function of the FADD-CASPASE-8-cFLIPL complex. Cell Rep. 1, 401-407 (2012).
    • (2012) Cell Rep , vol.1 , pp. 401-407
    • Dillon, C.P.1
  • 149
    • 52149095957 scopus 로고    scopus 로고
    • Mutation of a self-processing site in caspase-8 compromises its apoptotic but not its nonapoptotic functions in bacterial artificial chromosome- transgenic mice
    • Kang, T. B. et al. Mutation of a self-processing site in caspase-8 compromises its apoptotic but not its nonapoptotic functions in bacterial artificial chromosome-transgenic mice. J. Immunol. 181, 2522-2532 (2008).
    • (2008) J. Immunol , vol.181 , pp. 2522-2532
    • Kang, T.B.1
  • 150
    • 79952780505 scopus 로고    scopus 로고
    • Functional complementation between FADD and RIP1 in embryos and lymphocytes
    • Zhang, H. et al. Functional complementation between FADD and RIP1 in embryos and lymphocytes. Nature 471, 373-376 (2011).
    • (2011) Nature , vol.471 , pp. 373-376
    • Zhang, H.1
  • 151
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-κB signal
    • DOI 10.1016/S1074-7613(00)80535-X
    • Kelliher, M. A. et al. The death domain kinase RIP mediates the TNF-induced NF-.B signal. Immunity 8, 297-303 (1998). (Pubitemid 28188890)
    • (1998) Immunity , vol.8 , Issue.3 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3    Kuo, F.4    Stanger, B.Z.5    Leder, P.6
  • 152
    • 84961291582 scopus 로고    scopus 로고
    • RIPK1 both positively and negatively regulates RIPK3 oligomerization and necroptosis
    • Orozco, S. et al. RIPK1 both positively and negatively regulates RIPK3 oligomerization and necroptosis. Cell Death Differ. http://dx.doi.org/10.1038/ cdd.2014.76 (2014).
    • (2014) Cell Death Differ
    • Orozco, S.1
  • 153
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • DOI 10.1016/S0092-8674(03)00521-X
    • Micheau, O. & Tschopp, J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114, 181-190 (2003). (Pubitemid 36936912)
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 155
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach, B. et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471, 591-596 (2011).
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1
  • 156
    • 84864389178 scopus 로고    scopus 로고
    • NEMO inhibits programmed necrosis in an NF.Bindependent manner by restraining RIP1
    • O'Donnell, M. A., Hase, H., Legarda, D. & Ting, A. T. NEMO inhibits programmed necrosis in an NF.Bindependent manner by restraining RIP1. PloS ONE 7, e41238 (2012).
    • (2012) PloS ONE , vol.7
    • O'Donnell, M.A.1    Hase, H.2    Legarda, D.3    Ting, A.T.4
  • 157
    • 43049152912 scopus 로고    scopus 로고
    • TNF-α Induces Two Distinct Caspase-8 Activation Pathways
    • DOI 10.1016/j.cell.2008.03.036, PII S0092867408005011
    • Wang, L., Du, F. & Wang, X. TNF-a induces two distinct caspase-8 activation pathways. Cell 133, 693-703 (2008). (Pubitemid 351636305)
    • (2008) Cell , vol.133 , Issue.4 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 158
    • 84856160569 scopus 로고    scopus 로고
    • Caspase 8 inhibits programmed necrosis by processing CYLD
    • O'Donnell, M. A. et al. Caspase 8 inhibits programmed necrosis by processing CYLD. Nature Cell Biol. 13, 1437-1442 (2011).
    • (2011) Nature Cell Biol , vol.13 , pp. 1437-1442
    • O'Donnell, M.A.1
  • 159
    • 84867902828 scopus 로고    scopus 로고
    • Modulation of immune signalling by inhibitors of apoptosis
    • Beug, S. T., Cheung, H. H., LaCasse, E. C. & Korneluk, R. G. Modulation of immune signalling by inhibitors of apoptosis. Trends Immunol. 33, 535-545 (2012).
    • (2012) Trends Immunol , vol.33 , pp. 535-545
    • Beug, S.T.1    Cheung, H.H.2    Lacasse, E.C.3    Korneluk, R.G.4
  • 160
    • 4444243683 scopus 로고    scopus 로고
    • A small molecule smac mimic potentiates TRAIL- and TNFα-mediated cell death
    • DOI 10.1126/science.1098231
    • Li, L. et al. A small molecule Smac mimic potentiates TRAIL-and TNFa-mediated cell death. Science 305, 1471-1474 (2004). (Pubitemid 39167668)
    • (2004) Science , vol.305 , Issue.5689 , pp. 1471-1474
    • Li, L.1    Thomas, R.M.2    Suzuki, H.3    De Brabander, J.K.4    Wang, X.5    Harran, P.G.6
  • 161
    • 74049136127 scopus 로고    scopus 로고
    • Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type i interferons and proinflammatory cytokines
    • Tseng, P. H. et al. Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines. Nature Immunol. 11, 70-75 (2010).
    • (2010) Nature Immunol , vol.11 , pp. 70-75
    • Tseng, P.H.1
  • 162
    • 84862994793 scopus 로고    scopus 로고
    • Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response
    • Jiang, X. et al. Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response. Immunity 36, 959-973 (2012).
    • (2012) Immunity , vol.36 , pp. 959-973
    • Jiang, X.1
  • 163
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng, W. et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 141, 315-330 (2010).
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.1
  • 164
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou, F. et al. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146, 448-461 (2011).
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1
  • 165
    • 84898747432 scopus 로고    scopus 로고
    • Structural basis for the prion-like MAVS filaments in antiviral innate immunity
    • Xu, H. et al. Structural basis for the prion-like MAVS filaments in antiviral innate immunity. Elife 3, e01489 (2014).
    • (2014) Elife , vol.3
    • Xu, H.1
  • 166
    • 58049217490 scopus 로고    scopus 로고
    • RNA recognition and signal transduction by RIG-I-like receptors
    • Yoneyama, M. & Fujita, T. RNA recognition and signal transduction by RIG-I-like receptors. Immunol. Rev. 227, 54-65 (2009).
    • (2009) Immunol. Rev , vol.227 , pp. 54-65
    • Yoneyama, M.1    Fujita, T.2
  • 168
    • 84906571225 scopus 로고    scopus 로고
    • Inflammatory caspases are innate immune receptors for intracellular LPS
    • Shi, J. et al. Inflammatory caspases are innate immune receptors for intracellular LPS. Nature http://dx.doi.org/10.1038/nature13683 (2014).
    • (2014) Nature
    • Shi, J.1


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