메뉴 건너뛰기




Volumn 526, Issue 7575, 2015, Pages 666-671

Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 11; CRYOPYRIN; CYTOPLASM PROTEIN; ESCHERICHIA COLI LIPOPOLYSACCHARIDE; ETHYLNITROSOUREA; GASDERMIN D; INFLAMMASOME; INTERLEUKIN 1BETA; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; CASP11 PROTEIN, MOUSE; CASPASE; GSDMD PROTEIN, HUMAN; GSDMD PROTEIN, MOUSE; LIPOPOLYSACCHARIDE; TUMOR PROTEIN;

EID: 84942856523     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature15541     Document Type: Article
Times cited : (2663)

References (48)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 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
  • 4
    • 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
  • 5
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors asc and ipaf
    • Mariathasan S., et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218 (2004
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1
  • 6
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • Mariathasan S., et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440, 228-232 (2006
    • (2006) Nature , vol.440 , pp. 228-232
    • Mariathasan, S.1
  • 7
    • 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
  • 8
    • 84883790050 scopus 로고    scopus 로고
    • Cytoplasmic lps activates caspase-11: Implications intlr4-independent endotoxic shock
    • Hagar J. A., Powell D. A., Aachoui Y., Ernst R. K., & Miao E. A. Cytoplasmic LPS activates caspase-11: implications inTLR4-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
  • 9
    • 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 514, 187-192 (2014
    • (2014) Nature , vol.514 , pp. 187-192
    • Shi, J.1
  • 10
    • 0034813659 scopus 로고    scopus 로고
    • Genome-wide enumutagenesis to reveal immune regulators
    • Nelms K. A., & Goodnow C. C. Genome-wide ENUmutagenesis to reveal immune regulators. Immunity 15, 409-418 (2001
    • (2001) Immunity , vol.15 , pp. 409-418
    • Nelms, K.A.1    Goodnow, C.C.2
  • 11
    • 84907270863 scopus 로고    scopus 로고
    • Innate immune sensing of bacterial modifications of rho gtpases by the pyrin inflammasome
    • Xu H., et al. Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome. Nature 513, 237-241 (2014
    • (2014) Nature , vol.513 , pp. 237-241
    • Xu, H.1
  • 12
    • 16644363033 scopus 로고    scopus 로고
    • Identification and characterization of human dfna5l, mouse dfna5l, and rat dfna5l genes in silico
    • Katoh M., & Katoh M. Identification and characterization of human DFNA5L, mouse Dfna5l, and rat Dfna5l genes in silico. Int. J. Oncol. 25, 765-770 (2004
    • (2004) Int. J. Oncol , vol.25 , pp. 765-770
    • Katoh, M.1    Katoh, M.2
  • 13
    • 52049086465 scopus 로고    scopus 로고
    • Gasdermin d (gsdmd) is dispensable formouse intestinal epithelium development
    • Fujii T., et al. Gasdermin D (Gsdmd) is dispensable formouse intestinal epithelium development. Genesis 46, 418-423 (2008
    • (2008) Genesis , vol.46 , pp. 418-423
    • Fujii, T.1
  • 14
    • 34247217928 scopus 로고    scopus 로고
    • Members of a novel gene family, gsdm, are expressed exclusively in the epithelium of the skin and gastrointestinal tract in a highly tissue-specific manner
    • Tamura M., et al. Members of a novel gene family, Gsdm, are expressed exclusively in the epithelium of the skin and gastrointestinal tract in a highly tissue-specific manner. Genomics 89, 618-629 (2007
    • (2007) Genomics , vol.89 , pp. 618-629
    • Tamura, M.1
  • 15
    • 60749104535 scopus 로고    scopus 로고
    • Hin-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • Roberts T. L., et al. HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science 323, 1057-1060 (2009
    • (2009) Science , vol.323 , pp. 1057-1060
    • Roberts, T.L.1
  • 16
    • 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
  • 17
    • 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 458, 514-518 (2009
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1
  • 18
    • 33744464740 scopus 로고    scopus 로고
    • Cytosolic flagellin requires ipaf for activation of caspase-1 and interleukin 1b in salmonella-infected macrophages
    • Franchi L., et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1b in salmonella-infected macrophages. Nature Immunol. 7, 576-582 (2006
    • (2006) Nature Immunol , vol.7 , pp. 576-582
    • Franchi, L.1
  • 19
    • 76249108958 scopus 로고    scopus 로고
    • Listeria monocytogenes-infected human peripheral blood mononuclear cells produce il-1b, depending on listeriolysin o and nlrp3
    • Meixenberger K., et al. Listeria monocytogenes-infected human peripheral blood mononuclear cells produce IL-1b, depending on listeriolysin O and NLRP3. J. Immunol. 184, 922-930 (2010
    • (2010) J. Immunol , vol.184 , pp. 922-930
    • Meixenberger, K.1
  • 20
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder K., & Tschopp J. The inflammasomes. Cell 140, 821-832 (2010
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 21
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the nalp3 inflammasome
    • Martinon F., Petrilli V., Mayor A., Tardivel A., & Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237-241 (2006
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 22
    • 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. Nature Immunol. 9, 847-856 (2008
    • (2008) Nature Immunol , vol.9 , pp. 847-856
    • Hornung, V.1
  • 23
    • 37549041954 scopus 로고    scopus 로고
    • Immune recognition of pseudomonas aeruginosa mediated by the ipaf/nlrc4 inflammasome
    • Sutterwala F. S., et al. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. J. Exp. Med. 204, 3235-3245 (2007
    • (2007) J. Exp. Med , vol.204 , pp. 3235-3245
    • Sutterwala, F.S.1
  • 24
    • 84930225289 scopus 로고    scopus 로고
    • Human caspase-4 mediates noncanonical inflammasome activation against gram-negative bacterial pathogens
    • Casson C. N., et al. Human caspase-4 mediates noncanonical inflammasome activation against gram-negative bacterial pathogens. Proc. Natl Acad. Sci. USA 112, 6688-6693 (2015
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 6688-6693
    • Casson, C.N.1
  • 25
    • 62349098335 scopus 로고    scopus 로고
    • Caspases: Evolutionary aspects of their functions in vertebrates
    • Sakamaki K., & Satou Y. Caspases: evolutionary aspects of their functions in vertebrates. J. Fish Biol. 74, 727-753 (2009
    • (2009) J. Fish Biol , vol.74 , pp. 727-753
    • Sakamaki, K.1    Satou, Y.2
  • 26
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A., & Dixit V. M. Death receptors: signaling and modulation. Science 281, 1305-1308 (1998
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 27
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family andgranzyme b functional relationships establishedfor key mediators of apoptosis
    • Thornberry N. A., et al. A combinatorial approach defines specificities of members of the caspase family andgranzyme B. Functional relationships establishedfor key mediators of apoptosis. J. Biol. Chem. 272, 17907-17911 (1997
    • (1997) J. Biol. Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1
  • 28
    • 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
  • 29
    • 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
  • 30
    • 84943200249 scopus 로고    scopus 로고
    • Caspase-11 activates a canonical nlrp3 inflammasome by promoting k1 efflux
    • Rü hl S., & Broz P. Caspase-11 activates a canonical NLRP3 inflammasome by promoting K1 efflux. Eur. J. Immunol. http://dx.doi.org/10.1002/eji.201545772 (2015
    • (2015) Eur. J. Immunol
    • Rühl, S.1    Broz, P.2
  • 31
    • 77951805919 scopus 로고    scopus 로고
    • Inflammatory stimuli regulate caspase substrate profiles
    • Agard N. J., Maltby D., & Wells J. A. Inflammatory stimuli regulate caspase substrate profiles. Mol. Cell. Proteomics 9, 880-893 (2010
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 880-893
    • Agard, N.J.1    Maltby, D.2    Wells, J.A.3
  • 32
    • 84864868585 scopus 로고    scopus 로고
    • Evolution of inflammasome functions in vertebrates: Inflammasome and caspase-1 trigger fish macrophage cell death but are dispensable for the processing of IL-1b
    • Angosto D., et al. Evolution of inflammasome functions in vertebrates: Inflammasome and caspase-1 trigger fish macrophage cell death but are dispensable for the processing of IL-1b. Innate Immun. 18, 815-824 (2012
    • (2012) Innate Immun , vol.18 , pp. 815-824
    • Angosto, D.1
  • 33
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
    • Thornberry N. A., et al. A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356, 768-774 (1992
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1
  • 34
    • 68649102975 scopus 로고    scopus 로고
    • Mechanisms of interleukin-1b release
    • Eder C. Mechanisms of interleukin-1b release. Immunobiology 214, 543-553 (2009
    • (2009) Immunobiology , vol.214 , pp. 543-553
    • Eder, C.1
  • 35
    • 84908356704 scopus 로고    scopus 로고
    • Single-cell imaging of caspase-1 dynamics reveals an all-or-none inflammasome signaling response
    • Liu T., et al. Single-cell imaging of caspase-1 dynamics reveals an all-or-none inflammasome signaling response. Cell Rep. 8, 974-982 (2014
    • (2014) Cell Rep , vol.8 , pp. 974-982
    • Liu, T.1
  • 36
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ice-interacting protease, is essential for the activation of ice
    • Wang S., et al. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92, 501-509 (1998
    • (1998) Cell , vol.92 , pp. 501-509
    • Wang, S.1
  • 37
    • 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. Nature Immunol. 11, 1136-1142 (2010
    • (2010) Nature Immunol , vol.11 , pp. 1136-1142
    • Miao, E.A.1
  • 39
    • 84904743254 scopus 로고    scopus 로고
    • Edwardsiella tarda-induced cytotoxicity depends on its type III secretion system and flagellin
    • Xie H. X., et al. Edwardsiella tarda-induced cytotoxicity depends on its type III secretion system and flagellin. Infect. Immun. 82, 3436-3445 (2014
    • (2014) Infect. Immun , vol.82 , pp. 3436-3445
    • Xie, H.X.1
  • 40
    • 84897102291 scopus 로고    scopus 로고
    • Caspase-11 controls interleukin-1b release through degradation of trpc1
    • Py B. F., et al. Caspase-11 controls interleukin-1b release through degradation of TRPC1. Cell Rep. 6, 1122-1128 (2014
    • (2014) Cell Rep , vol.6 , pp. 1122-1128
    • Py, B.F.1
  • 41
    • 84864232091 scopus 로고    scopus 로고
    • Massively parallel sequencing of the mouse exome to accurately identify rare, inducedmutations: Animmediate source for thousands of new mouse models
    • Andrews T. D., et al. Massively parallel sequencing of the mouse exome to accurately identify rare, inducedmutations: animmediate source for thousands of new mouse models. Open Biol. 2, 120061 (2012
    • (2012) Open Biol , vol.2 , pp. 120061
    • Andrews, T.D.1
  • 43
    • 18244379035 scopus 로고    scopus 로고
    • Identification of cpt a, a pmra-regulated locus required for phosphoethanolamine modification of the salmonella enterica serovar typhimurium lipopolysaccharide core
    • Tamayo R., et al. Identification of cpt A, a PmrA-regulated locus required for phosphoethanolamine modification of the Salmonella enterica serovar typhimurium lipopolysaccharide core. J. Bacteriol. 187, 3391-3399 (2005
    • (2005) J. Bacteriol , vol.187 , pp. 3391-3399
    • Tamayo, R.1
  • 44
    • 0000369624 scopus 로고
    • A method for the determination of amino acid sequence in peptides
    • Edman P. A method for the determination of amino acid sequence in peptides. Arch. Biochem. 22, 475 (1949
    • (1949) Arch. Biochem , vol.22 , pp. 475
    • Edman, P.1
  • 45
    • 0033081238 scopus 로고    scopus 로고
    • Protein identification using20-minuteEdman cycles and sequence mixture analysis
    • Henzel W. J., Tropea J., & Dupont D. Protein identification using20-minuteEdman cycles and sequence mixture analysis. Anal. Biochem. 267, 148-160 (1999
    • (1999) Anal. Biochem , vol.267 , pp. 148-160
    • Henzel, W.J.1    Tropea, J.2    Dupont, D.3
  • 46
    • 33645318751 scopus 로고    scopus 로고
    • Quantitative production of macrophages or neutrophils ex vivo using conditional hoxb8
    • Wang G. G., et al. Quantitative production of macrophages or neutrophils ex vivo using conditional Hoxb8. Nature Methods 3, 287-293 (2006
    • (2006) Nature Methods , vol.3 , pp. 287-293
    • Wang, G.G.1
  • 47
    • 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 490, 539-542 (2012
    • (2012) Nature , vol.490 , pp. 539-542
    • Qu, Y.1
  • 48
    • 78751706713 scopus 로고    scopus 로고
    • Hoxb8 conditionally immortalised macrophage lines model inflammatory monocytic cells with important similarity to dendritic cells
    • Rosas M., et al. Hoxb8 conditionally immortalised macrophage lines model inflammatory monocytic cells with important similarity to dendritic cells. Eur. J. Immunol. 41, 356-365 (2011
    • (2011) Eur. J. Immunol , vol.41 , pp. 356-365
    • Rosas, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.