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Volumn 34, Issue 2, 2013, Pages 41-49

Caspases and immunity in a deadly grip

Author keywords

Apoptosis; Caspase; Immunity; Inflammation; Necroptosis

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE 11; CASPASE 8; CRYOPYRIN; CYTOCHROME C; FLAGELLIN; HIGH MOBILITY GROUP B1 PROTEIN; INFLAMMASOME; INITIATION FACTOR 2ALPHA; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; REACTIVE OXYGEN METABOLITE; THIOREDOXIN INTERACTING PROTEIN; VOLTAGE DEPENDENT ANION CHANNEL 1; X LINKED INHIBITOR OF APOPTOSIS;

EID: 84873186300     PISSN: 14714906     EISSN: 14714981     Source Type: Journal    
DOI: 10.1016/j.it.2012.09.005     Document Type: Review
Times cited : (16)

References (96)
  • 1
    • 39749182234 scopus 로고    scopus 로고
    • Apoptosis: controlled demolition at the cellular level
    • Taylor R.C., et al. Apoptosis: controlled demolition at the cellular level. Nat. Rev. Mol. Cell Biol. 2008, 9:231-234.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 231-234
    • Taylor, R.C.1
  • 2
    • 44349111132 scopus 로고    scopus 로고
    • Caspase activity mediates the differentiation of embryonic stem cells
    • Fujita J., et al. Caspase activity mediates the differentiation of embryonic stem cells. Cell Stem Cell 2008, 2:595-601.
    • (2008) Cell Stem Cell , vol.2 , pp. 595-601
    • Fujita, J.1
  • 3
    • 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. 2008, 181:2522-2532.
    • (2008) J. Immunol. , vol.181 , pp. 2522-2532
    • Kang, T.B.1
  • 4
    • 0038284956 scopus 로고    scopus 로고
    • Caspase-mediated processing of the Drosophila NF-kappaB factor Relish
    • Stoven S., et al. Caspase-mediated processing of the Drosophila NF-kappaB factor Relish. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:5991-5996.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5991-5996
    • Stoven, S.1
  • 5
    • 40449097257 scopus 로고    scopus 로고
    • The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response
    • Muruve D.A., et al. The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response. Nature 2008, 452:103-107.
    • (2008) Nature , vol.452 , pp. 103-107
    • Muruve, D.A.1
  • 6
    • 66749174867 scopus 로고    scopus 로고
    • The inflammasomes: guardians of the body
    • Martinon F., et al. The inflammasomes: guardians of the body. Annu. Rev. Immunol. 2009, 27:229-265.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 229-265
    • Martinon, F.1
  • 7
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T., et al. AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 2009, 458:509-513.
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1
  • 8
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • Hornung V., et al. AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature 2009, 458:514-518.
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1
  • 9
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • Bürckstümmer T., et al. An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat. Immunol. 2009, 10:266-272.
    • (2009) Nat. Immunol. , vol.10 , pp. 266-272
    • Bürckstümmer, T.1
  • 10
    • 79956061094 scopus 로고    scopus 로고
    • IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi sarcoma-associated herpesvirus infection
    • Kerur N., et al. IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi sarcoma-associated herpesvirus infection. Cell Host Microbe 2011, 9:363-375.
    • (2011) Cell Host Microbe , vol.9 , pp. 363-375
    • Kerur, N.1
  • 11
    • 74049126045 scopus 로고    scopus 로고
    • Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production
    • Poeck H., et al. Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production. Nat. Immunol. 2010, 11:63-69.
    • (2010) Nat. Immunol. , vol.11 , pp. 63-69
    • Poeck, H.1
  • 12
    • 69549119940 scopus 로고    scopus 로고
    • Molecular mechanisms involved in inflammasome activation
    • Bryant C., Fitzgerald K.A. Molecular mechanisms involved in inflammasome activation. Trends Cell Biol. 2009, 19:455-464.
    • (2009) Trends Cell Biol. , vol.19 , pp. 455-464
    • Bryant, C.1    Fitzgerald, K.A.2
  • 13
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • Halle A., et al. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat. Immunol. 2008, 9:857-865.
    • (2008) Nat. Immunol. , vol.9 , pp. 857-865
    • Halle, A.1
  • 14
    • 43249125839 scopus 로고    scopus 로고
    • Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
    • Dostert C., et al. Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 2008, 320:674-677.
    • (2008) Science , vol.320 , pp. 674-677
    • Dostert, C.1
  • 15
    • 75649096002 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein links oxidative stress to inflammasome activation
    • Zhou R., et al. Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat. Immunol. 2010, 11:136-140.
    • (2010) Nat. Immunol. , vol.11 , pp. 136-140
    • Zhou, R.1
  • 16
    • 77956958947 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1b in type 2 diabetes
    • Masters S.L., et al. Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1b in type 2 diabetes. Nat. Immunol. 2010, 11:897-904.
    • (2010) Nat. Immunol. , vol.11 , pp. 897-904
    • Masters, S.L.1
  • 17
    • 79551584144 scopus 로고    scopus 로고
    • Hyperglycemia activates caspase-1 and TXNIP-mediated IL-1beta transcription in human adipose tissue
    • Koenen T.B., et al. Hyperglycemia activates caspase-1 and TXNIP-mediated IL-1beta transcription in human adipose tissue. Diabetes 2011, 60:517-524.
    • (2011) Diabetes , vol.60 , pp. 517-524
    • Koenen, T.B.1
  • 18
    • 77954312028 scopus 로고    scopus 로고
    • Inflammasome activation. The missing link: how the inflammasome senses oxidative stress
    • Jin C., Flavell R.A. Inflammasome activation. The missing link: how the inflammasome senses oxidative stress. Immunol. Cell Biol. 2010, 88:510-512.
    • (2010) Immunol. Cell Biol. , vol.88 , pp. 510-512
    • Jin, C.1    Flavell, R.A.2
  • 19
    • 81355146675 scopus 로고    scopus 로고
    • Interplay between redox status and inflammasome activation
    • Rubartelli A., et al. Interplay between redox status and inflammasome activation. Trends Immunol. 2011, 32:559-566.
    • (2011) Trends Immunol. , vol.32 , pp. 559-566
    • Rubartelli, A.1
  • 20
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed E.M., Vance R.E. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 2011, 477:592-595.
    • (2011) Nature , vol.477 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 21
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • Zhao Y., et al. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 2011, 477:596-600.
    • (2011) Nature , vol.477 , pp. 596-600
    • Zhao, Y.1
  • 22
    • 84860225554 scopus 로고    scopus 로고
    • GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals
    • Shenoy A.R., et al. GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals. Science 2012, 336:481-485.
    • (2012) Science , vol.336 , pp. 481-485
    • Shenoy, A.R.1
  • 23
    • 84867861468 scopus 로고    scopus 로고
    • Phosphorylation of NLRC4 is critical for inflammasome activation
    • Qu Y., et al. Phosphorylation of NLRC4 is critical for inflammasome activation. Nature 2012, 490:539-542.
    • (2012) Nature , vol.490 , pp. 539-542
    • Qu, Y.1
  • 24
    • 84865511926 scopus 로고    scopus 로고
    • Novel role of PKR in inflammasome activation and HMGB1 release
    • Lu B., et al. Novel role of PKR in inflammasome activation and HMGB1 release. Nature 2012, 488:670-674.
    • (2012) Nature , vol.488 , pp. 670-674
    • Lu, B.1
  • 25
    • 0343852938 scopus 로고    scopus 로고
    • Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways
    • Wong A.H., et al. Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways. EMBO J. 1997, 16:1291-1304.
    • (1997) EMBO J. , vol.16 , pp. 1291-1304
    • Wong, A.H.1
  • 26
    • 84861442790 scopus 로고    scopus 로고
    • Regulation of actin dynamics by protein kinase R control of gelsolin enforces basal innate immune defense
    • Irving A.T., et al. Regulation of actin dynamics by protein kinase R control of gelsolin enforces basal innate immune defense. Immunity 2012, 36:795-806.
    • (2012) Immunity , vol.36 , pp. 795-806
    • Irving, A.T.1
  • 27
    • 79957576718 scopus 로고    scopus 로고
    • NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis
    • Elinav E., et al. NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis. Cell 2011, 145:745-757.
    • (2011) Cell , vol.145 , pp. 745-757
    • Elinav, E.1
  • 28
    • 84858796861 scopus 로고    scopus 로고
    • An NLRP7-containing inflammasome mediates recognition of microbial lipopeptides in human macrophages
    • Khare S., et al. An NLRP7-containing inflammasome mediates recognition of microbial lipopeptides in human macrophages. Immunity 2012, 36:464-476.
    • (2012) Immunity , vol.36 , pp. 464-476
    • Khare, S.1
  • 29
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R., et al. A role for mitochondria in NLRP3 inflammasome activation. Nature 2011, 469:221-225.
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1
  • 30
    • 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 2012, 36:401-414.
    • (2012) Immunity , vol.36 , pp. 401-414
    • Shimada, K.1
  • 31
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • Nakahira K., et al. Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat. Immunol. 2011, 12:222-230.
    • (2011) Nat. Immunol. , vol.12 , pp. 222-230
    • Nakahira, K.1
  • 32
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • Saitoh T., et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature 2008, 456:264-268.
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1
  • 33
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1b production by targeting ubiquitinated inflammasomes for destruction
    • Shi C.S., et al. Activation of autophagy by inflammatory signals limits IL-1b production by targeting ubiquitinated inflammasomes for destruction. Nat. Immunol. 2012, 13:255-263.
    • (2012) Nat. Immunol. , vol.13 , pp. 255-263
    • Shi, C.S.1
  • 34
    • 80055021939 scopus 로고    scopus 로고
    • Adenovirus type 5 rupture of lysosomes leads to cathepsin B-dependent mitochondrial stress and production of reactive oxygen species
    • McGuire K.A., et al. Adenovirus type 5 rupture of lysosomes leads to cathepsin B-dependent mitochondrial stress and production of reactive oxygen species. J. Virol. 2011, 85:10806-10813.
    • (2011) J. Virol. , vol.85 , pp. 10806-10813
    • McGuire, K.A.1
  • 35
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • Hornung V., et al. Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat. Immunol. 2008, 9:847-856.
    • (2008) Nat. Immunol. , vol.9 , pp. 847-856
    • Hornung, V.1
  • 36
    • 84866156921 scopus 로고    scopus 로고
    • Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome
    • Ito M., et al. Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome. PLoS Pathog. 2012, 8:e1002857.
    • (2012) PLoS Pathog. , vol.8
    • Ito, M.1
  • 37
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1
  • 38
    • 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. Nat. Rev. Mol. Cell Biol. 2010, 11:621-632.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 39
    • 84857175933 scopus 로고    scopus 로고
    • Dectin-1 is an extracellular pathogen sensor for the induction and processing of IL-1?. 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-1?. via a noncanonical caspase-8 inflammasome. Nat. Immunol. 2012, 13:246-254.
    • (2012) Nat. Immunol. , vol.13 , pp. 246-254
    • Gringhuis, S.I.1
  • 40
    • 51049100571 scopus 로고    scopus 로고
    • Stimulation of Toll-like receptor 3 and 4 induces interleukin-1beta maturation by caspase-8
    • Maelfait J., et al. Stimulation of Toll-like receptor 3 and 4 induces interleukin-1beta maturation by caspase-8. J. Exp. Med. 2008, 205:1967-1973.
    • (2008) J. Exp. Med. , vol.205 , pp. 1967-1973
    • Maelfait, J.1
  • 41
    • 84866087868 scopus 로고    scopus 로고
    • AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages. Cell Death Differ. (in press)
    • Pierini, R. et al. (2012) AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages. Cell Death Differ. (in press).
    • (2012)
    • Pierini, R.1
  • 42
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • Kayagaki N., et al. Non-canonical inflammasome activation targets caspase-11. Nature 2011, 479:117-121.
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1
  • 43
    • 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 2012, 150:606-619.
    • (2012) Cell , vol.150 , pp. 606-619
    • Rathinam, V.A.1
  • 44
    • 0034704161 scopus 로고    scopus 로고
    • Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-gamma
    • Lin X.Y., et al. Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-gamma. J. Biol. Chem. 2000, 275:39920-39926.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39920-39926
    • Lin, X.Y.1
  • 45
    • 2542457495 scopus 로고    scopus 로고
    • Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory disease
    • Martinon F., Tschopp J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory disease. Cell 2004, 117:561-574.
    • (2004) Cell , vol.117 , pp. 561-574
    • Martinon, F.1    Tschopp, J.2
  • 46
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F., et al. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol. Cell 2002, 10:417-426.
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1
  • 47
    • 84856832054 scopus 로고    scopus 로고
    • Caspase-4 is required for activation of inflammasomes
    • Sollberger G., et al. Caspase-4 is required for activation of inflammasomes. J. Immunol. 2012, 188:1992-2000.
    • (2012) J. Immunol. , vol.188 , pp. 1992-2000
    • Sollberger, G.1
  • 48
    • 84864292536 scopus 로고    scopus 로고
    • Caspase-11 promotes the fusion of phagosomes harboring pathogenic bacteria with lysosomes by modulating actin polymerization
    • Akhter A., et al. Caspase-11 promotes the fusion of phagosomes harboring pathogenic bacteria with lysosomes by modulating actin polymerization. Immunity 2012, 37:35-47.
    • (2012) Immunity , vol.37 , pp. 35-47
    • Akhter, A.1
  • 49
    • 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. 1995, 14:1914-1922.
    • (1995) EMBO J. , vol.14 , pp. 1914-1922
    • Faucheu, C.1
  • 50
    • 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 2012, 490:288-291.
    • (2012) Nature , vol.490 , pp. 288-291
    • Broz, P.1
  • 51
    • 84859464225 scopus 로고    scopus 로고
    • An inactivating caspase 11 passenger mutation originating from the 129 murine strain in mice targeted for c-IAP1
    • Kenneth N.S., et al. An inactivating caspase 11 passenger mutation originating from the 129 murine strain in mice targeted for c-IAP1. Biochem. J. 2012, 443:355-359.
    • (2012) Biochem. J. , vol.443 , pp. 355-359
    • Kenneth, N.S.1
  • 52
    • 77951628300 scopus 로고    scopus 로고
    • Caspase-1 independent IL-1beta production is critical for host resistance to mycobacterium tuberculosis and does not require TLR signaling in vivo
    • Mayer-Barber K.D., et al. Caspase-1 independent IL-1beta production is critical for host resistance to mycobacterium tuberculosis and does not require TLR signaling in vivo. J. Immunol. 2010, 184:3326-3330.
    • (2010) J. Immunol. , vol.184 , pp. 3326-3330
    • Mayer-Barber, K.D.1
  • 53
    • 84857166396 scopus 로고    scopus 로고
    • A new path to IL-1b production controlled by caspase-8
    • Dupaul-Chicoine J., Saleh M. A new path to IL-1b production controlled by caspase-8. Nat. Immunol. 2012, 13:211-212.
    • (2012) Nat. Immunol. , vol.13 , pp. 211-212
    • Dupaul-Chicoine, J.1    Saleh, M.2
  • 54
    • 77954930632 scopus 로고    scopus 로고
    • IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer
    • Gyrd-Hansen M., Meier P. IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer. Nat. Rev. Cancer 2010, 10:561-574.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 561-574
    • Gyrd-Hansen, M.1    Meier, P.2
  • 55
    • 55949118522 scopus 로고    scopus 로고
    • Inactivation of effector caspases through nondegradative polyubiquitylation
    • Ditzel M., et al. Inactivation of effector caspases through nondegradative polyubiquitylation. Mol. Cell 2008, 32:540-553.
    • (2008) Mol. Cell , vol.32 , pp. 540-553
    • Ditzel, M.1
  • 56
    • 80053439574 scopus 로고    scopus 로고
    • Drosophila IAP1-mediated ubiquitylation controls activation of the initiator caspase DRONC independent of protein degradation
    • Lee T.V., et al. Drosophila IAP1-mediated ubiquitylation controls activation of the initiator caspase DRONC independent of protein degradation. PLoS Genet. 2011, 7:e1002261.
    • (2011) PLoS Genet. , vol.7
    • Lee, T.V.1
  • 57
    • 79959539790 scopus 로고    scopus 로고
    • Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death
    • Vucic D., et al. Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death. Nat. Rev. Mol. Cell Biol. 2011, 12:439-452.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 439-452
    • Vucic, D.1
  • 58
    • 65549160961 scopus 로고    scopus 로고
    • The CULt of caspase-8 ubiquitination
    • Békés M., Salvesen G.S. The CULt of caspase-8 ubiquitination. Cell 2009, 137:604-606.
    • (2009) Cell , vol.137 , pp. 604-606
    • Békés, M.1    Salvesen, G.S.2
  • 59
    • 84255178199 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis proteins cIAP1 and cIAP2 are required for efficient caspase-1 activation by the inflammasome
    • Labbé K., et al. Cellular inhibitors of apoptosis proteins cIAP1 and cIAP2 are required for efficient caspase-1 activation by the inflammasome. Immunity 2011, 35:897-907.
    • (2011) Immunity , vol.35 , pp. 897-907
    • Labbé, K.1
  • 60
    • 65549085701 scopus 로고    scopus 로고
    • Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling
    • Jin Z., et al. Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling. Cell 2009, 137:721-735.
    • (2009) Cell , vol.137 , pp. 721-735
    • Jin, Z.1
  • 61
    • 84862189464 scopus 로고    scopus 로고
    • Ubiquitylation of the initiator caspase DREDD is required for innate immune signalling
    • Meinander A., et al. Ubiquitylation of the initiator caspase DREDD is required for innate immune signalling. EMBO J. 2012, 31:2770-2783.
    • (2012) EMBO J. , vol.31 , pp. 2770-2783
    • Meinander, A.1
  • 62
    • 79955484976 scopus 로고    scopus 로고
    • The spatial and temporal organization of ubiquitin networks
    • Grabbe C., et al. The spatial and temporal organization of ubiquitin networks. Nat. Rev. Mol. Cell Biol. 2011, 12:295-307.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 295-307
    • Grabbe, C.1
  • 63
    • 80052754179 scopus 로고    scopus 로고
    • Caspase-1 promiscuity is counterbalanced by rapid inactivation of processed enzyme
    • Walsh J.G., et al. Caspase-1 promiscuity is counterbalanced by rapid inactivation of processed enzyme. J. Biol. Chem. 2011, 286:32513-32524.
    • (2011) J. Biol. Chem. , vol.286 , pp. 32513-32524
    • Walsh, J.G.1
  • 64
    • 84863009653 scopus 로고    scopus 로고
    • Patched dependence receptor triggers apoptosis through ubiquitination of caspase-9
    • Fombonne J., et al. Patched dependence receptor triggers apoptosis through ubiquitination of caspase-9. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:10510-10515.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 10510-10515
    • Fombonne, J.1
  • 65
    • 79960224920 scopus 로고    scopus 로고
    • Molecular determinants of Smac mimetic induced degradation of cIAP1 and cIAP2
    • Darding M., et al. Molecular determinants of Smac mimetic induced degradation of cIAP1 and cIAP2. Cell Death Differ. 2011, 18:1376-1386.
    • (2011) Cell Death Differ. , vol.18 , pp. 1376-1386
    • Darding, M.1
  • 66
    • 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 2011, 36:215-227.
    • (2011) Immunity , vol.36 , pp. 215-227
    • Vince, J.E.1
  • 67
    • 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 2011, 43:432-448.
    • (2011) Mol. Cell , vol.43 , pp. 432-448
    • Tenev, T.1
  • 68
    • 82455212812 scopus 로고    scopus 로고
    • 'Necrosome'-induced inflammation: must cells die for it?
    • Wallach D., et al. 'Necrosome'-induced inflammation: must cells die for it?. Trends Immunol. 2011, 32:505-509.
    • (2011) Trends Immunol. , vol.32 , pp. 505-509
    • Wallach, D.1
  • 69
    • 84867902828 scopus 로고    scopus 로고
    • Modulation of immune signalling by inhibitors of apoptosis
    • Beug S.T., et al. Modulation of immune signalling by inhibitors of apoptosis. Trends Immunol. 2012, 33:535-545.
    • (2012) Trends Immunol. , vol.33 , pp. 535-545
    • Beug, S.T.1
  • 70
    • 84857433477 scopus 로고    scopus 로고
    • Inhibitors of apoptosis proteins and IL-1b: a tangled relationship
    • Ciraci C., Sutterwala F.S. Inhibitors of apoptosis proteins and IL-1b: a tangled relationship. Immunity 2012, 36:155-157.
    • (2012) Immunity , vol.36 , pp. 155-157
    • Ciraci, C.1    Sutterwala, F.S.2
  • 71
    • 78449269290 scopus 로고    scopus 로고
    • Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
    • Miao E.A., et al. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat. Immunol. 2010, 11:1136-1142.
    • (2010) Nat. Immunol. , vol.11 , pp. 1136-1142
    • Miao, E.A.1
  • 72
    • 84860668802 scopus 로고    scopus 로고
    • Lethal inflammasome activation by a multidrug-resistant pathobiont upon antibiotic disruption of the microbiota
    • Ayres J.S., et al. Lethal inflammasome activation by a multidrug-resistant pathobiont upon antibiotic disruption of the microbiota. Nat. Med. 2012, 18:799-806.
    • (2012) Nat. Med. , vol.18 , pp. 799-806
    • Ayres, J.S.1
  • 73
    • 67349124914 scopus 로고    scopus 로고
    • Immunogenic and tolerogenic cell death
    • Green D.R., et al. Immunogenic and tolerogenic cell death. Nat. Rev. Immunol. 2009, 9:353-363.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 353-363
    • Green, D.R.1
  • 74
    • 84861435630 scopus 로고    scopus 로고
    • A perspective on mammalian caspases as positive and negative regulators of inflammation
    • Martin S.J., et al. A perspective on mammalian caspases as positive and negative regulators of inflammation. Mol. Cell 2012, 46:387-397.
    • (2012) Mol. Cell , vol.46 , pp. 387-397
    • Martin, S.J.1
  • 75
    • 68249137289 scopus 로고    scopus 로고
    • Suppression of interleukin-33 bioactivity through proteolysis by apoptotic caspases
    • Lüthi A.U., et al. Suppression of interleukin-33 bioactivity through proteolysis by apoptotic caspases. Immunity 2009, 31:84-98.
    • (2009) Immunity , vol.31 , pp. 84-98
    • Lüthi, A.U.1
  • 76
    • 46749136790 scopus 로고    scopus 로고
    • Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein
    • Kazama H., et al. Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein. Immunity 2008, 29:21-32.
    • (2008) Immunity , vol.29 , pp. 21-32
    • Kazama, H.1
  • 77
    • 80052845560 scopus 로고    scopus 로고
    • Caspase-8 regulates TNF-α-induced epithelial necroptosis and terminal ileitis
    • Günther C., et al. Caspase-8 regulates TNF-α-induced epithelial necroptosis and terminal ileitis. Nature 2011, 477:335-339.
    • (2011) Nature , vol.477 , pp. 335-339
    • Günther, C.1
  • 78
    • 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. 2009, 206:2161-2177.
    • (2009) J. Exp. Med. , vol.206 , pp. 2161-2177
    • Kovalenko, A.1
  • 79
    • 68049092912 scopus 로고    scopus 로고
    • RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway
    • Chiu Y.H., et al. RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell 2009, 138:576-591.
    • (2009) Cell , vol.138 , pp. 576-591
    • Chiu, Y.H.1
  • 80
    • 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 2011, 34:340-351.
    • (2011) Immunity , vol.34 , pp. 340-351
    • Rajput, A.1
  • 81
    • 80052989433 scopus 로고    scopus 로고
    • Caspase-8-mediated cleavage inhibits IRF-3 protein by facilitating its proteasome-mediated degradation
    • Sears N., et al. Caspase-8-mediated cleavage inhibits IRF-3 protein by facilitating its proteasome-mediated degradation. J. Biol. Chem. 2011, 286:33037-33044.
    • (2011) J. Biol. Chem. , vol.286 , pp. 33037-33044
    • Sears, N.1
  • 82
    • 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 2011, 471:368-372.
    • (2011) Nature , vol.471 , pp. 368-372
    • Kaiser, W.J.1
  • 83
    • 80755132824 scopus 로고    scopus 로고
    • The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation
    • Bonnet M.C., et al. The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation. Immunity 2011, 35:572-582.
    • (2011) Immunity , vol.35 , pp. 572-582
    • Bonnet, M.C.1
  • 84
    • 80052850704 scopus 로고    scopus 로고
    • FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation
    • Welz P.S., et al. FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation. Nature 2011, 477:330-334.
    • (2011) Nature , vol.477 , pp. 330-334
    • Welz, P.S.1
  • 85
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis
    • Oberst A., et al. Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis. Nature 2011, 471:363-367.
    • (2011) Nature , vol.471 , pp. 363-367
    • Oberst, A.1
  • 86
    • 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. Nat. Cell Biol. 2011, 13:1437-1442.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1437-1442
    • O'Donnell, M.A.1
  • 87
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination
    • Kovalenko A., et al. The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. Nature 2003, 424:801-805.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1
  • 88
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • Feng S., et al. Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell. Signal. 2007, 19:2056-2067.
    • (2007) Cell. Signal. , vol.19 , pp. 2056-2067
    • Feng, S.1
  • 89
    • 0037160117 scopus 로고    scopus 로고
    • The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex
    • Micheau O., et al. The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex. J. Biol. Chem. 2002, 277:45162-45171.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45162-45171
    • Micheau, O.1
  • 90
    • 76149104286 scopus 로고    scopus 로고
    • Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment
    • Geserick P., et al. Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment. J. Cell Biol. 2009, 187:1037-1054.
    • (2009) J. Cell Biol. , vol.187 , pp. 1037-1054
    • Geserick, P.1
  • 91
    • 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 2011, 43:449-463.
    • (2011) Mol. Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1
  • 92
    • 80053580530 scopus 로고    scopus 로고
    • RIPK-dependent necrosis and its regulation by caspases: a mystery in five acts
    • Green D.R., et al. RIPK-dependent necrosis and its regulation by caspases: a mystery in five acts. Mol. Cell 2011, 44:9-16.
    • (2011) Mol. Cell , vol.44 , pp. 9-16
    • Green, D.R.1
  • 93
    • 79960110569 scopus 로고    scopus 로고
    • Programmed necrosis from molecules to health and disease
    • Galluzzi L., et al. Programmed necrosis from molecules to health and disease. Int. Rev. Cell Mol. Biol. 2011, 289:1-35.
    • (2011) Int. Rev. Cell Mol. Biol. , vol.289 , pp. 1-35
    • Galluzzi, L.1
  • 94
    • 84856231635 scopus 로고    scopus 로고
    • Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways
    • Mocarski E.S., et al. Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways. Nat. Rev. Immunol. 2011, 12:79-88.
    • (2011) Nat. Rev. Immunol. , vol.12 , pp. 79-88
    • Mocarski, E.S.1
  • 95
    • 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 2009, 137:1112-1123.
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1
  • 96
    • 77954593965 scopus 로고    scopus 로고
    • Virus inhibition of RIP3-dependent necrosis
    • Upton J.W., et al. Virus inhibition of RIP3-dependent necrosis. Cell Host Microbe 2010, 7:302-313.
    • (2010) Cell Host Microbe , vol.7 , pp. 302-313
    • Upton, J.W.1


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