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Volumn 8, Issue 4, 2012, Pages

Proteolytic processing of Nlrp1b is required for inflammasome activity

Author keywords

[No Author keywords available]

Indexed keywords

INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; LACTATE DEHYDROGENASE; NLRP1B PROTEIN; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; TOXIN; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; NALP1B PROTEIN, MOUSE;

EID: 84861215715     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002659     Document Type: Article
Times cited : (127)

References (29)
  • 1
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T, Yu JW, Datta P, Wu J, Alnemri ES, (2009) AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 458: 509-513.
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 2
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • Hornung V, Ablasser A, Charrel-Dennis M, Bauernfeind F, Horvath G, et al. (2009) AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature 458: 514-518.
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1    Ablasser, A.2    Charrel-Dennis, M.3    Bauernfeind, F.4    Horvath, G.5
  • 3
    • 60749104535 scopus 로고    scopus 로고
    • HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • Roberts TL, Idris A, Dunn JA, Kelly GM, Burnton CM, et al. (2009) HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science 323: 1057-1060.
    • (2009) Science , vol.323 , pp. 1057-1060
    • Roberts, T.L.1    Idris, A.2    Dunn, J.A.3    Kelly, G.M.4    Burnton, C.M.5
  • 4
    • 47849085872 scopus 로고    scopus 로고
    • The NALP3 inflammasome is involved in the innate immune response to amyloid-beta
    • Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, et al. (2008) The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol 9: 857-865.
    • (2008) Nat Immunol , vol.9 , pp. 857-865
    • Halle, A.1    Hornung, V.2    Petzold, G.C.3    Stewart, C.R.4    Monks, B.G.5
  • 5
    • 47849097202 scopus 로고    scopus 로고
    • Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
    • Hornung V, Bauernfeind F, Halle A, Samstad EO, Kono H, et al. (2008) Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol 9: 847-856.
    • (2008) Nat Immunol , vol.9 , pp. 847-856
    • Hornung, V.1    Bauernfeind, F.2    Halle, A.3    Samstad, E.O.4    Kono, H.5
  • 6
    • 77649179433 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production?
    • Tschopp J, Schroder K, (2010) NLRP3 inflammasome activation: The convergence of multiple signalling pathways on ROS production? Nat Rev Immunol 10: 210-215.
    • (2010) Nat Rev Immunol , vol.10 , pp. 210-215
    • Tschopp, J.1    Schroder, K.2
  • 7
    • 79960542894 scopus 로고    scopus 로고
    • Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome
    • Bauernfeind F, Bartok E, Rieger A, Franchi L, Nunez G, et al. Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol 187: 613-617.
    • J Immunol , vol.187 , pp. 613-617
    • Bauernfeind, F.1    Bartok, E.2    Rieger, A.3    Franchi, L.4    Nunez, G.5
  • 8
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed EM, Vance RE, (2011) Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature 477: 592-595.
    • (2011) Nature , vol.477 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 9
    • 80053349020 scopus 로고    scopus 로고
    • The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
    • Zhao Y, Yang J, Shi J, Gong YN, Lu Q, et al. (2011) The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature 477: 596-600.
    • (2011) Nature , vol.477 , pp. 596-600
    • Zhao, Y.1    Yang, J.2    Shi, J.3    Gong, Y.N.4    Lu, Q.5
  • 10
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J, (2002) The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 10: 417-426.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 11
    • 70349413074 scopus 로고    scopus 로고
    • Expression of Nlrp1b inflammasome components in human fibroblasts confers susceptibility to anthrax lethal toxin
    • Liao KC, Mogridge J, (2009) Expression of Nlrp1b inflammasome components in human fibroblasts confers susceptibility to anthrax lethal toxin. Infect Immun 77: 4455-4462.
    • (2009) Infect Immun , vol.77 , pp. 4455-4462
    • Liao, K.C.1    Mogridge, J.2
  • 12
    • 33847376042 scopus 로고    scopus 로고
    • Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation
    • Faustin B, Lartigue L, Bruey JM, Luciano F, Sergienko E, et al. (2007) Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation. Mol Cell 25: 713-724.
    • (2007) Mol Cell , vol.25 , pp. 713-724
    • Faustin, B.1    Lartigue, L.2    Bruey, J.M.3    Luciano, F.4    Sergienko, E.5
  • 13
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • Boyden ED, Dietrich WF, (2006) Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat Genet 38: 240-244.
    • (2006) Nat Genet , vol.38 , pp. 240-244
    • Boyden, E.D.1    Dietrich, W.F.2
  • 14
    • 36349019887 scopus 로고    scopus 로고
    • Proteasomes control caspase-1 activation in anthrax lethal toxin-mediated cell killing
    • Squires RC, Muehlbauer SM, Brojatsch J, (2007) Proteasomes control caspase-1 activation in anthrax lethal toxin-mediated cell killing. J Biol Chem 282: 34260-34267.
    • (2007) J Biol Chem , vol.282 , pp. 34260-34267
    • Squires, R.C.1    Muehlbauer, S.M.2    Brojatsch, J.3
  • 15
    • 38049119726 scopus 로고    scopus 로고
    • Anthrax lethal toxin-induced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome
    • Wickliffe KE, Leppla SH, Moayeri M, (2008) Anthrax lethal toxin-induced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome. Cell Microbiol 10: 332-343.
    • (2008) Cell Microbiol , vol.10 , pp. 332-343
    • Wickliffe, K.E.1    Leppla, S.H.2    Moayeri, M.3
  • 16
    • 70849088615 scopus 로고    scopus 로고
    • Anthrax lethal toxin induced lysosomal membrane permeabilization and cytosolic cathepsin release is Nlrp1b/Nalp1b-dependent
    • Averette KM, Pratt MR, Yang Y, Bassilian S, Whitelegge JP, et al. (2009) Anthrax lethal toxin induced lysosomal membrane permeabilization and cytosolic cathepsin release is Nlrp1b/Nalp1b-dependent. PLoS One 4: e7913.
    • (2009) PLoS One , vol.4
    • Averette, K.M.1    Pratt, M.R.2    Yang, Y.3    Bassilian, S.4    Whitelegge, J.P.5
  • 17
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: receptor binding, internalization, pore formation, and translocation
    • Young JA, Collier RJ, (2007) Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu Rev Biochem 76: 243-265.
    • (2007) Annu Rev Biochem , vol.76 , pp. 243-265
    • Young, J.A.1    Collier, R.J.2
  • 18
    • 79955036655 scopus 로고    scopus 로고
    • The unfolding story of anthrax toxin translocation
    • Thoren KL, Krantz BA, (2011) The unfolding story of anthrax toxin translocation. Mol Microbiol 80: 588-595.
    • (2011) Mol Microbiol , vol.80 , pp. 588-595
    • Thoren, K.L.1    Krantz, B.A.2
  • 19
    • 70350482699 scopus 로고    scopus 로고
    • Cellular and systemic effects of anthrax lethal toxin and edema toxin
    • Moayeri M, Leppla SH, (2009) Cellular and systemic effects of anthrax lethal toxin and edema toxin. Mol Aspects Med 30: 439-455.
    • (2009) Mol Aspects Med , vol.30 , pp. 439-455
    • Moayeri, M.1    Leppla, S.H.2
  • 20
    • 41949127121 scopus 로고    scopus 로고
    • Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms
    • Fink SL, Bergsbaken T, Cookson BT, (2008) Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Proc Natl Acad Sci U S A 105: 4312-4317.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4312-4317
    • Fink, S.L.1    Bergsbaken, T.2    Cookson, B.T.3
  • 21
    • 73949099407 scopus 로고    scopus 로고
    • Cutting edge: resistance to Bacillus anthracis infection mediated by a lethal toxin sensitive allele of Nalp1b/Nlrp1b
    • Terra JK, Cote CK, France B, Jenkins AL, Bozue JA, et al. (2010) Cutting edge: resistance to Bacillus anthracis infection mediated by a lethal toxin sensitive allele of Nalp1b/Nlrp1b. J Immunol 184: 17-20.
    • (2010) J Immunol , vol.184 , pp. 17-20
    • Terra, J.K.1    Cote, C.K.2    France, B.3    Jenkins, A.L.4    Bozue, J.A.5
  • 22
    • 78651258397 scopus 로고    scopus 로고
    • Inflammasome sensor Nlrp1b-dependent resistance to anthrax is mediated by caspase-1, IL-1 signaling and neutrophil recruitment
    • Moayeri M, Crown D, Newman ZL, Okugawa S, Eckhaus M, et al. (2010) Inflammasome sensor Nlrp1b-dependent resistance to anthrax is mediated by caspase-1, IL-1 signaling and neutrophil recruitment. PLoS Pathog 6: e1001222.
    • (2010) PLoS Pathog , vol.6
    • Moayeri, M.1    Crown, D.2    Newman, Z.L.3    Okugawa, S.4    Eckhaus, M.5
  • 24
    • 33846219997 scopus 로고    scopus 로고
    • Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway
    • Tinel A, Janssens S, Lippens S, Cuenin S, Logette E, et al. (2007) Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway. EMBO J 26: 197-208.
    • (2007) EMBO J , vol.26 , pp. 197-208
    • Tinel, A.1    Janssens, S.2    Lippens, S.3    Cuenin, S.4    Logette, E.5
  • 25
    • 33751217186 scopus 로고    scopus 로고
    • Monitoring regulated protein-protein interactions using split TEV
    • Wehr MC, Laage R, Bolz U, Fischer TM, Grunewald S, et al. (2006) Monitoring regulated protein-protein interactions using split TEV. Nat Methods 3: 985-993.
    • (2006) Nat Methods , vol.3 , pp. 985-993
    • Wehr, M.C.1    Laage, R.2    Bolz, U.3    Fischer, T.M.4    Grunewald, S.5
  • 26
    • 0024708229 scopus 로고
    • Molecular genetic analysis of a plant virus polyprotein cleavage site: a model
    • Dougherty WG, Cary SM, Parks TD, (1989) Molecular genetic analysis of a plant virus polyprotein cleavage site: a model. Virology 171: 356-364.
    • (1989) Virology , vol.171 , pp. 356-364
    • Dougherty, W.G.1    Cary, S.M.2    Parks, T.D.3
  • 27
    • 59649103157 scopus 로고    scopus 로고
    • Wheel of Life, Wheel of Death: A Mechanistic Insight into Signaling by STAND Proteins
    • Danot O, Marquenet E, Vidal-Ingigliardi D, Richet E, (2009) Wheel of Life, Wheel of Death: A Mechanistic Insight into Signaling by STAND Proteins. Structure 17: 172-182.
    • (2009) Structure , vol.17 , pp. 172-182
    • Danot, O.1    Marquenet, E.2    Vidal-Ingigliardi, D.3    Richet, E.4
  • 28
    • 13844318262 scopus 로고    scopus 로고
    • Differentiation of human monocytic cell lines confers susceptibility to Bacillus anthracis lethal toxin
    • Kassam A, Der SD, Mogridge J, (2005) Differentiation of human monocytic cell lines confers susceptibility to Bacillus anthracis lethal toxin. Cell Microbiol 7: 281-292.
    • (2005) Cell Microbiol , vol.7 , pp. 281-292
    • Kassam, A.1    der, S.D.2    Mogridge, J.3
  • 29
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust RB, Tozser J, Fox JD, Anderson DE, Cherry S, et al. (2001) Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng 14: 993-1000.
    • (2001) Protein Eng , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.