메뉴 건너뛰기




Volumn 12, Issue 12, 2012, Pages 833-844

The role of the IAP E3 ubiquitin ligases in regulating pattern-recognition receptor signalling

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; CASPASE RECRUITMENT DOMAIN PROTEIN 4; INFLAMMASOME; INHIBITOR OF APOPTOSIS PROTEIN; INTERLEUKIN 1BETA CONVERTING ENZYME; PATTERN RECOGNITION RECEPTOR; RETINOIC ACID INDUCIBLE PROTEIN I; TOLL LIKE RECEPTOR; UBIQUITIN PROTEIN LIGASE E3;

EID: 84870242006     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri3325     Document Type: Review
Times cited : (62)

References (109)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 82955249021 scopus 로고    scopus 로고
    • Nod-like receptors and the innate immune system: Coping with danger, damage and death
    • Kersse, K., Bertrand, M. J., Lamkanfi, M. & Vandenabeele, P. NOD-like receptors and the innate immune system: coping with danger, damage and death. Cytokine Growth Factor Rev. 22, 257-276 (2011).
    • (2011) Cytokine Growth Factor Rev , vol.22 , pp. 257-276
    • Kersse, K.1    Bertrand, M.J.2    Lamkanfi, M.3    Vandenabeele, P.4
  • 4
    • 84655176306 scopus 로고    scopus 로고
    • The role of ubiquitylation in immune defence and pathogen evasion
    • Jiang, X. & Chen, Z. J. The role of ubiquitylation in immune defence and pathogen evasion. Nature Rev. Immunol. 12, 35-48 (2012).
    • (2012) Nature Rev. Immunol , vol.12 , pp. 35-48
    • Jiang, X.1    Chen, Z.J.2
  • 5
    • 66149086936 scopus 로고    scopus 로고
    • Nod-like receptors: Role in innate immunity and inflammatory disease
    • Chen, G., Shaw, M. H., Kim, Y. G. & Nunez, G. NOD-like receptors: role in innate immunity and inflammatory disease. Annu. Rev. Pathol. 4, 365-398 (2009).
    • (2009) Annu. Rev. Pathol , vol.4 , pp. 365-398
    • Chen, G.1    Shaw, M.H.2    Kim, Y.G.3    Nunez, G.4
  • 6
    • 46249124976 scopus 로고    scopus 로고
    • Deubiquitylation and regulation of the immune response
    • Sun, S. C. Deubiquitylation and regulation of the immune response. Nature Rev. Immunol. 8, 501-511 (2008).
    • (2008) Nature Rev. Immunol , vol.8 , pp. 501-511
    • Sun, S.C.1
  • 7
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander, D. The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37, 937-953 (2009).
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 937-953
    • Komander, D.1
  • 9
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • DOI 10.1038/40901
    • Deveraux, Q. L., Takahashi, R., Salvesen, G. S. & Reed, J. C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388, 300-304 (1997). (Pubitemid 27317977)
    • (1997) Nature , vol.388 , Issue.6639 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 10
    • 43049091895 scopus 로고    scopus 로고
    • IAPs: What's in a Name?
    • DOI 10.1016/j.molcel.2008.03.008, PII S1097276508002086
    • Srinivasula, S. M. & Ashwell, J. D. IAPs: what's in a name? Mol. Cell 30, 123-135 (2008). (Pubitemid 351626688)
    • (2008) Molecular Cell , vol.30 , Issue.2 , pp. 123-135
    • Srinivasula, S.M.1    Ashwell, J.D.2
  • 11
    • 77954930632 scopus 로고    scopus 로고
    • Iaps: From caspase inhibitors to modulators of nf-κb, inflammation and cancer
    • Gyrd-Hansen, M. & Meier, P. IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer. Nature Rev. Cancer 10, 561-574 (2010).
    • (2010) Nature Rev. Cancer , vol.10 , pp. 561-574
    • Gyrd-Hansen, M.1    Meier, P.2
  • 12
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • DOI 10.1126/science.288.5467.874
    • Yang, Y., Fang, S., Jensen, J. P., Weissman, A. M. & Ashwell, J. D. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288, 874-877 (2000). (Pubitemid 30257739)
    • (2000) Science , vol.288 , Issue.5467 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 13
    • 79952623655 scopus 로고    scopus 로고
    • Ciap1 and tak1 protect cells from tnf-induced necrosis by preventing rip1/rip3-dependent reactive oxygen species production
    • Vanlangenakker, N. et al. cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production. Cell Death Differ. 18, 656-665 (2011).
    • (2011) Cell Death Differ , vol.18 , pp. 656-665
    • Vanlangenakker, N.1
  • 14
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to tnf-α
    • He, S. et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α. Cell 137, 1100-1111 (2009).
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 15
    • 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. 187, 1037-1054 (2009).
    • (2009) J. Cell Biol , vol.187 , pp. 1037-1054
    • Geserick, P.1
  • 16
    • 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
  • 17
    • 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
  • 21
    • 84858627919 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis are global regulators of nf-κb and mapk activation by members of the tnf family of receptors
    • Varfolomeev, E. et al. Cellular inhibitors of apoptosis are global regulators of NF-κB and MAPK activation by members of the TNF family of receptors. Sci. Signal. 5, ra22 (2012).
    • (2012) Sci. Signal , vol.5
    • Varfolomeev, E.1
  • 22
    • 54049155149 scopus 로고    scopus 로고
    • C-iap1 and c-iap2 are critical mediators of tumor necrosis factor α (tnfα)-induced nf-κb activation
    • Varfolomeev, E. et al. c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor α (TNFα)-induced NF-κB activation. J. Biol. Chem. 283, 24295-24299 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 24295-24299
    • Varfolomeev, E.1
  • 23
    • 50149121101 scopus 로고    scopus 로고
    • Both ciap1 and ciap2 regulate tnfα-mediated nf-κb activation
    • Mahoney, D. J. et al. Both cIAP1 and cIAP2 regulate TNFα-mediated NF-κB activation. Proc. Natl Acad. Sci. USA 105, 11778-11783 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 11778-11783
    • Mahoney, D.J.1
  • 24
    • 84859424337 scopus 로고    scopus 로고
    • Iaps limit activation of rip kinases by tnf receptor 1 during development
    • Moulin, M. et al. IAPs limit activation of RIP kinases by TNF receptor 1 during development. EMBO J. 31, 1679-1691 (2012).
    • (2012) EMBO J , vol.31 , pp. 1679-1691
    • Moulin, M.1
  • 25
    • 66949138341 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis ciap1 and ciap2 are required for innate immunity signaling by the pattern recognition receptors nod1 and nod2
    • Bertrand, M. J. et al. Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2. Immunity 30, 789-801 (2009).
    • (2009) Immunity , vol.30 , pp. 789-801
    • Bertrand, M.J.1
  • 26
    • 84863000898 scopus 로고    scopus 로고
    • The ubiquitin ligase xiap recruits lubac for nod2 signaling in inflammation and innate immunity
    • This study provides the first evidence for non-redundant ubiquitylation-dependent functions of cIAP1 and cIAP2 in NOD1 and NOD2 signalling by functioning as K63 ubiquitin ligases for RIPK2
    • This study provides the first evidence for non-redundant ubiquitylation-dependent functions of cIAP1 and cIAP2 in NOD1 and NOD2 signalling by functioning as K63 ubiquitin ligases for RIPK2. 26. Damgaard, R. B. et al. The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling in inflammation and innate immunity. Mol. Cell 46, 746-758 (2012).
    • (2012) Mol. Cell , vol.46 , pp. 746-758
  • 27
    • 70149099161 scopus 로고    scopus 로고
    • Xiap mediates nod signaling via interaction with rip2
    • This paper shows that XIAP positively regulates NOD2-mediated immunity by promoting RIPK2 ubiquitylation and by inducing recruitment of LUBAC to the receptor-signalling complex
    • This paper shows that XIAP positively regulates NOD2-mediated immunity by promoting RIPK2 ubiquitylation and by inducing recruitment of LUBAC to the receptor-signalling complex. 27. Krieg, A. et al. XIAP mediates NOD signaling via interaction with RIP2. Proc. Natl Acad. Sci. USA 106, 14524-14529 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14524-14529
    • Krieg, A.1
  • 28
    • 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
  • 29
    • 77951247349 scopus 로고    scopus 로고
    • Virus-triggered ubiquitination of traf3/6 by ciap1/2 is essential for induction of interferon-β (ifn-β) and cellular antiviral response
    • This study demonstrates that cIAP1 and cIAP2-induced proteosomal degradation of TRAF3 is required for TLR4-mediated pro-inflammatory cytokine induction by facilitating translocation of the MYD88 complex to the cytosol where it activates MAPK signalling pathways
    • This study demonstrates that cIAP1 and cIAP2-induced proteosomal degradation of TRAF3 is required for TLR4-mediated pro-inflammatory cytokine induction by facilitating translocation of the MYD88 complex to the cytosol where it activates MAPK signalling pathways. 29. Mao, A. P. et al. Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-β (IFN-β) and cellular antiviral response. J. Biol. Chem. 285, 9470-9476 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 9470-9476
    • Mao, A.P.1
  • 30
    • 84255178199 scopus 로고    scopus 로고
    • Cellular inhibitors of apoptosis proteins ciap1 and ciap2 are required for efficient caspase-1 activation by the inflammasome
    • Labb, K., McIntire, C. R., Doiron, K., Leblanc, P. M. & Saleh, M. Cellular inhibitors of apoptosis proteins cIAP1 and cIAP2 are required for efficient caspase-1 activation by the inflammasome. Immunity 35, 897-907 (2011).
    • (2011) Immunity , vol.35 , pp. 897-907
    • Labb, K.1    McIntire, C.R.2    Doiron, K.3    Leblanc, P.M.4    Saleh, M.5
  • 31
    • 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
  • 32
    • 80053602333 scopus 로고    scopus 로고
    • The regulation of tnf signalling: What a tangled web we weave
    • References 30 and 31 provide contrasting evidence for a role of XIAP, cIAP1 and cIAP2 in inflammasome activation and pro-IL-1β processing
    • References 30 and 31 provide contrasting evidence for a role of XIAP, cIAP1 and cIAP2 in inflammasome activation and pro-IL-1β processing. 32. Silke, J. The regulation of TNF signalling: what a tangled web we weave. Curr. Opin. Immunol. 23, 620-626 (2011).
    • (2011) Curr. Opin. Immunol , vol.23 , pp. 620-626
    • Silke, J.1
  • 33
    • 79959539790 scopus 로고    scopus 로고
    • Ubiquitylation in apoptosis: A post-translational modification at the edge of life and death
    • Vucic, D., Dixit, V. M. & Wertz, I. E. Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death. Nature Rev. Mol. Cell Biol. 12, 439-452 (2011).
    • (2011) Nature Rev. Mol. Cell Biol , vol.12 , pp. 439-452
    • Vucic, D.1    Dixit, V.M.2    Wertz, I.E.3
  • 34
    • 0027537461 scopus 로고
    • An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif
    • Crook, N. E., Clem, R. J. & Miller, L. K. An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif. J. Virol. 67, 2168-2174 (1993). (Pubitemid 23088392)
    • (1993) Journal of Virology , vol.67 , Issue.4 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 35
    • 33645640920 scopus 로고    scopus 로고
    • The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases
    • DOI 10.1074/jbc.M510863200
    • Eckelman, B. P. & Salvesen, G. S. The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases. J. Biol. Chem. 281, 3254-3260 (2006). (Pubitemid 43845937)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3254-3260
    • Eckelman, B.P.1    Salvesen, G.S.2
  • 36
    • 33749252583 scopus 로고    scopus 로고
    • Human inhibitor of apoptosis proteins: Why XIAP is the black sheep of the family
    • DOI 10.1038/sj.embor.7400795, PII 7400795
    • Eckelman, B. P., Salvesen, G. S. & Scott, F. L. Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family. EMBO Rep. 7, 988-994 (2006). (Pubitemid 44480512)
    • (2006) EMBO Reports , vol.7 , Issue.10 , pp. 988-994
    • Eckelman, B.P.1    Salvesen, G.S.2    Scott, F.L.3
  • 37
    • 67649794805 scopus 로고    scopus 로고
    • The e3 ubiquitin ligase ciap1 binds and ubiquitinates caspase-3 and -7 via unique mechanisms at distinct steps in their processing
    • Choi, Y. E. et al. The E3 ubiquitin ligase cIAP1 binds and ubiquitinates caspase-3 and -7 via unique mechanisms at distinct steps in their processing. J. Biol. Chem. 284, 12772-12782 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 12772-12782
    • Choi, Y.E.1
  • 38
    • 58249086500 scopus 로고    scopus 로고
    • Ubiquitin binding modulates iap antagonist-stimulated proteasomal degradation of c-iap1 and c-iap2
    • Blankenship, J. W. et al. Ubiquitin binding modulates IAP antagonist-stimulated proteasomal degradation of c-IAP1 and c-IAP2. Biochem. J. 417, 149-160 (2009).
    • (2009) Biochem. J , vol.417 , pp. 149-160
    • Blankenship, J.W.1
  • 39
    • 55549140475 scopus 로고    scopus 로고
    • Iaps contain an evolutionarily conserved ubiquitin-binding domain that regulates nf-κb as well as cell survival and oncogenesis
    • Gyrd-Hansen, M. et al. IAPs contain an evolutionarily conserved ubiquitin-binding domain that regulates NF-κB as well as cell survival and oncogenesis. Nature Cell Biol. 10, 1309-1317 (2008).
    • (2008) Nature Cell Biol , vol.10 , pp. 1309-1317
    • Gyrd-Hansen, M.1
  • 40
    • 79958051518 scopus 로고    scopus 로고
    • Card-mediated autoinhibition of ciap1's e3 ligase activity suppresses cell proliferation and migration
    • Lopez, J. et al. CARD-mediated autoinhibition of cIAP1's E3 ligase activity suppresses cell proliferation and migration. Mol. Cell 42, 569-583 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 569-583
    • Lopez, J.1
  • 41
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • DOI 10.1146/annurev.immunol.25.022106.141615
    • Lemaitre, B. & Hoffmann, J. The host defense of Drosophila melanogaster. Annu. Rev. Immunol. 25, 697-743 (2007). (Pubitemid 46697922)
    • (2007) Annual Review of Immunology , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 42
    • 35549006674 scopus 로고    scopus 로고
    • The Drosophila systemic immune response: Sensing and signalling during bacterial and fungal infections
    • DOI 10.1038/nri2194, PII NRI2194
    • Ferrandon, D., Imler, J. L., Hetru, C. & Hoffmann, J. A. The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections. Nature Rev. Immunol. 7, 862-874 (2007). (Pubitemid 350006241)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.11 , pp. 862-874
    • Ferrandon, D.1    Imler, J.-L.2    Hetru, C.3    Hoffmann, J.A.4
  • 43
    • 34447628324 scopus 로고    scopus 로고
    • Iap2 is required for a sustained response in the Drosophila Imd pathway
    • DOI 10.1016/j.dci.2007.01.004, PII S0145305X07000092
    • Valanne, S., Kleino, A., Myllymaki, H., Vuoristo, J. & Ramet, M. Iap2 is required for a sustained response in the Drosophila Imd pathway. Dev. Comp. Immunol. 31, 991-1001 (2007). (Pubitemid 47095005)
    • (2007) Developmental and Comparative Immunology , vol.31 , Issue.10 , pp. 991-1001
    • Valanne, S.1    Kleino, A.2    Myllymaki, H.3    Vuoristo, J.4    Ramet, M.5
  • 44
    • 33847273186 scopus 로고    scopus 로고
    • The Drosophila inhibitor of apoptosis (IAP) DIAP2 is dispensable for cell survival, required for the innate immune response to Gram-negative bacterial infection, and can be negatively regulated by the Reaper/Hid/Grim family of IAP-binding apoptosis inducers
    • DOI 10.1074/jbc.M608051200
    • Huh, J. R. et al. The Drosophila inhibitor of apoptosis (IAP) DIAP2 is dispensable for cell survival, required for the innate immune response to gram-negative bacterial infection, and can be negatively regulated by the reaper/hid/grim family of IAP-binding apoptosis inducers. J. Biol. Chem. 282, 2056-2068 (2007). (Pubitemid 47076727)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 2056-2068
    • Huh, J.R.1    Foe, I.2    Muro, I.3    Chun, H.C.4    Jae, H.S.5    Soon, J.Y.6    Guo, M.7    Jin, M.P.8    Hay, B.A.9
  • 45
    • 33750330952 scopus 로고    scopus 로고
    • The Drosophila inhibitor of apoptosis protein DIAP2 functions in innate immunity and is essential to resist gram-negative bacterial infection
    • DOI 10.1128/MCB.00548-06
    • Leulier, F., Lhocine, N., Lemaitre, B. & Meier, P. The Drosophila inhibitor of apoptosis protein DIAP2 functions in innate immunity and is essential to resist gram-negative bacterial infection. Mol. Cell. Biol. 26, 7821-7831 (2006). (Pubitemid 44630984)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.21 , pp. 7821-7831
    • Leulier, F.1    Lhocine, N.2    Lemaitre, B.3    Meier, P.4
  • 47
    • 27344453240 scopus 로고    scopus 로고
    • An RNA interference screen identifies Inhibitor of Apoptosis Protein 2 as a regulator of innate immune signalling in Drosophila
    • DOI 10.1038/sj.embor.7400530, PII 7400530
    • Gesellchen, V., Kuttenkeuler, D., Steckel, M., Pelte, N. & Boutros, M. An RNA interference screen identifies Inhibitor of Apoptosis Protein 2 as a regulator of innate immune signalling in Drosophila. EMBO Rep. 6, 979-984 (2005). (Pubitemid 41521955)
    • (2005) EMBO Reports , vol.6 , Issue.10 , pp. 979-984
    • Gesellchen, V.1    Kuttenkeuler, D.2    Steckel, M.3    Pelte, N.4    Boutros, M.5
  • 48
    • 74749093547 scopus 로고    scopus 로고
    • Caspase-mediated cleavage, iap binding, and ubiquitination: Linking three mechanisms crucial for drosophila nf-κb signaling
    • References 45-47 provide the first in vitro and in vivo evidence for a role of an IAP (DIAP2) in the regulation of innate immune PRR (PGRP-LC) signalling
    • References 45-47 provide the first in vitro and in vivo evidence for a role of an IAP (DIAP2) in the regulation of innate immune PRR (PGRP-LC) signalling. 48. Paquette, N. et al. Caspase-mediated cleavage, IAP binding, and ubiquitination: linking three mechanisms crucial for Drosophila NF-κB signaling. Mol. Cell 37, 172-182 (2010).
    • (2010) Mol. Cell , vol.37 , pp. 172-182
    • Paquette, N.1
  • 49
    • 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. 31, 2770-2783 (2012).
    • (2012) EMBO J , vol.31 , pp. 2770-2783
    • Meinander, A.1
  • 50
    • 12844279852 scopus 로고    scopus 로고
    • Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor
    • DOI 10.1073/pnas.0404952102
    • References 48 and 49 provided the molecular mechanism accounting for the role of DIAP2 in the IMD pathway, which involves K63-linked ubiquitylation of IMD (reference 48) and DREDD (reference 49). IMD and DREDD are both required for PGRP-LC-induced innate immune responses. 50. Choe, K. M., Lee, H. & Anderson, K. V. Drosophila peptidoglycan recognition protein LC (PGRP-LC) acts as a signal-transducing innate immune receptor. Proc. Natl Acad. Sci. USA 102, 1122-1126 (2005). (Pubitemid 40170736)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.4 , pp. 1122-1126
    • Choe, K.-M.1    Lee, H.2    Anderson, K.V.3
  • 53
    • 0037172656 scopus 로고    scopus 로고
    • Inducible expression of double-stranded RNA reveals a role for dFADD in the regulation of the antibacterial response in Drosophila adults
    • DOI 10.1016/S0960-9822(02)00873-4, PII S0960982202008734
    • Leulier, F., Vidal, S., Saigo, K., Ueda, R. & Lemaitre, B. Inducible expression of double-stranded RNA reveals a role for dFADD in the regulation of the antibacterial response in Drosophila adults. Curr. Biol. 12, 996-1000 (2002). (Pubitemid 34703329)
    • (2002) Current Biology , vol.12 , Issue.12 , pp. 996-1000
    • Leulier, F.1    Vidal, S.2    Saigo, K.3    Ueda, R.4    Lemaitre, B.5
  • 54
    • 0034305744 scopus 로고    scopus 로고
    • The drosophila caspase dredd is required to resist gram-negative bacterial infection
    • Leulier, F., Rodriguez, A., Khush, R. S., Abrams, J. M. & Lemaitre, B. The Drosophila caspase Dredd is required to resist gram-negative bacterial infection. EMBO Rep. 1, 353-358 (2000).
    • (2000) EMBO Rep , vol.1 , pp. 353-358
    • Leulier, F.1    Rodriguez, A.2    Khush, R.S.3    Abrams, J.M.4    Lemaitre, B.5
  • 55
    • 0034700491 scopus 로고    scopus 로고
    • Structural basis of IAP recognition by Smac/DIABLO
    • DOI 10.1038/35050012
    • Wu, G. et al. Structural basis of IAP recognition by Smac/DIABLO. Nature 408, 1008-1012 (2000). (Pubitemid 32101651)
    • (2000) Nature , vol.408 , Issue.6815 , pp. 1008-1012
    • Wu, G.1    Chai, J.2    Suber, T.L.3    Wu, J.-W.4    Du, C.5    Wang, X.6    Shi, Y.7
  • 57
    • 33645099737 scopus 로고    scopus 로고
    • Drosophila tab2 is required for the immune activation of jnk and nf-κb
    • Zhuang, Z. H. et al. Drosophila TAB2 is required for the immune activation of JNK and NF-κB. Cell Signal 18, 964-970 (2006).
    • (2006) Cell Signal , vol.18 , pp. 964-970
    • Zhuang, Z.H.1
  • 58
    • 1542571463 scopus 로고    scopus 로고
    • Immune activation of nf-κb and jnk requires drosophila tak1
    • Silverman, N. et al. Immune activation of NF-κB and JNK requires Drosophila TAK1. J. Biol. Chem. 278, 48928-48934 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 48928-48934
    • Silverman, N.1
  • 59
    • 0035423794 scopus 로고    scopus 로고
    • Mutations in the drosophila dtak1 gene reveal a conserved function for mapkkks in the control of relnf-κb-dependent innate immune responses
    • Vidal, S. et al. Mutations in the Drosophila dTAK1 gene reveal a conserved function for MAPKKKs in the control of rel/NF-κB-dependent innate immune responses. Genes Dev. 15, 1900-1912 (2001).
    • (2001) Genes Dev , vol.15 , pp. 1900-1912
    • Vidal, S.1
  • 60
    • 0034287444 scopus 로고    scopus 로고
    • A drosophila iκb kinase complex required for relish cleavage and antibacterial immunity
    • Silverman, N. et al. A Drosophila IκB kinase complex required for Relish cleavage and antibacterial immunity. Genes Dev. 14, 2461-2471 (2000).
    • (2000) Genes Dev , vol.14 , pp. 2461-2471
    • Silverman, N.1
  • 61
    • 0034303573 scopus 로고    scopus 로고
    • Role of drosophila ikkγ in a toll-independent antibacterial immune response
    • Rutschmann, S. et al. Role of Drosophila IKKγ in a toll-independent antibacterial immune response. Nature Immunol. 1, 342-347 (2000).
    • (2000) Nature Immunol , vol.1 , pp. 342-347
    • Rutschmann, S.1
  • 62
    • 0035187882 scopus 로고    scopus 로고
    • The antibacterial arm of the Drosophila innate immune response requires an IκB kinase
    • DOI 10.1101/gad.856901
    • Lu, Y., Wu, L. P. & Anderson, K. V. The antibacterial arm of the Drosophila innate immune response requires an IκB kinase. Genes Dev. 15, 104-110 (2001). (Pubitemid 32060686)
    • (2001) Genes and Development , vol.15 , Issue.1 , pp. 104-110
    • Lu, Y.1    Wu, L.P.2    Anderson, K.V.3
  • 63
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of lys 63-linked polyubiquitination by nemo is a key event in nf-κb activation [corrected]
    • Wu, C. J., Conze, D. B., Li, T. Srinivasula, S. M. & Ashwell, J. D. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation [corrected]. Nature Cell Biol. 8, 398-406 (2006).
    • (2006) Nature Cell Biol , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 65
    • 70449597294 scopus 로고    scopus 로고
    • A non-redundant role for drosophila mkk4 and hemipterous/mkk7 in tak1-mediated activation of jnk
    • Geuking, P., Narasimamurthy, R., Lemaitre, B., Basler, K. & Leulier, F. A non-redundant role for Drosophila Mkk4 and hemipterous/Mkk7 in TAK1-mediated activation of JNK. PLoS ONE 4, e7709 (2009).
    • (2009) PLoS ONE , vol.4
    • Geuking, P.1    Narasimamurthy, R.2    Lemaitre, B.3    Basler, K.4    Leulier, F.5
  • 66
    • 67649858793 scopus 로고    scopus 로고
    • Two roles for the drosophila ikk complex in the activation of relish and the induction of antimicrobial peptide genes
    • Erturk-Hasdemir, D. et al. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Proc. Natl Acad. Sci. USA 106, 9779-9784 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 9779-9784
    • Erturk-Hasdemir, D.1
  • 67
    • 0034303480 scopus 로고    scopus 로고
    • Activation of the drosophila nf-κb factor relish by rapid endoproteolytic cleavage
    • Stoven, S., Ando, I., Kadalayil, L., Engstrom, Y. & Hultmark, D. Activation of the Drosophila NF-κB factor Relish by rapid endoproteolytic cleavage. EMBO Rep. 1, 347-352 (2000).
    • (2000) EMBO Rep , vol.1 , pp. 347-352
    • Stoven, S.1    Ando, I.2    Kadalayil, L.3    Engstrom, Y.4    Hultmark, D.5
  • 69
    • 72649083654 scopus 로고    scopus 로고
    • The drosophila ubiquitin-specific protease dusp36/scny targets imd to prevent constitutive immune signaling
    • Thevenon, D. et al. The Drosophila ubiquitin-specific protease dUSP36/Scny targets IMD to prevent constitutive immune signaling. Cell Host Microbe 6, 309-320 (2009).
    • (2009) Cell Host Microbe , vol.6 , pp. 309-320
    • Thevenon, D.1
  • 70
    • 34547754626 scopus 로고    scopus 로고
    • A Drosophila ortholog of the human cylindromatosis tumor suppressor gene regulates triglyceride content and antibacterial defense
    • DOI 10.1242/dev.02859
    • Tsichritzis, T. et al. A Drosophila ortholog of the human cylindromatosis tumor suppressor gene regulates triglyceride content and antibacterial defense. Development 134, 2605-2614 (2007). (Pubitemid 47225957)
    • (2007) Development , vol.134 , Issue.14 , pp. 2605-2614
    • Tsichritzis, T.1    Gaentzsch, P.C.2    Kosmidis, S.3    Brown, A.E.4    Skoulakis, E.M.5    Ligoxygakis, P.6    Mosialos, G.7
  • 71
    • 50849091946 scopus 로고    scopus 로고
    • Xiap regulates cytosol-specific innate immunity to listeria infection
    • Bauler, L. D., Duckett, C. S. & O'Riordan, M. X. XIAP regulates cytosol-specific innate immunity to Listeria infection. PLoS Pathog. 4, e1000142 (2008).
    • (2008) PLoS Pathog , vol.4
    • Bauler, L.D.1    Duckett, C.S.2    O'Riordan, M.X.3
  • 76
    • 0037075549 scopus 로고    scopus 로고
    • Involvement of receptor-interacting protein 2 in innate and adaptive immune responses
    • DOI 10.1038/416190a
    • Chin, A. I. et al. Involvement of receptor-interacting protein 2 in innate and adaptive immune responses. Nature 416, 190-194 (2002). (Pubitemid 34246478)
    • (2002) Nature , vol.416 , Issue.6877 , pp. 190-194
    • Chin, A.I.1    Dempsey, P.W.2    Bruhn, K.3    Miller, J.F.4    Xu, Y.5    Cheng, G.6
  • 77
    • 0033591330 scopus 로고    scopus 로고
    • Nod1, an apaf-1-like activator of caspase-9 and nuclear factor-κb
    • Inohara, N. et al. Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-κB. J. Biol. Chem. 274, 14560-14567 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 14560-14567
    • Inohara, N.1
  • 80
    • 37548999003 scopus 로고    scopus 로고
    • Nod2 pathway activation by mdp or mycobacterium tuberculosis infection involves the stable polyubiquitination of rip2
    • Yang, Y. et al. NOD2 pathway activation by MDP or Mycobacterium tuberculosis infection involves the stable polyubiquitination of Rip2. J. Biol. Chem. 282, 36223-36229 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 36223-36229
    • Yang, Y.1
  • 81
    • 80052638486 scopus 로고    scopus 로고
    • Ciap1/2 are direct e3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (rip1-4
    • Bertrand, M. J. et al. cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4). PLoS ONE 6, e22356 (2011).
    • (2011) PLoS ONE , vol.6
    • Bertrand, M.J.1
  • 83
    • 33846469538 scopus 로고    scopus 로고
    • The adaptor protein card9 is required for innate immune responses to intracellular pathogens
    • Hsu, Y. M. et al. The adaptor protein CARD9 is required for innate immune responses to intracellular pathogens. Nature Immunol. 8, 198-205 (2007).
    • (2007) Nature Immunol , vol.8 , pp. 198-205
    • Hsu, Y.M.1
  • 85
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by nemo is important for nf-κb activation
    • Rahighi, S. et al. Specific recognition of linear ubiquitin chains by NEMO is important for NF-κB activation. Cell 136, 1098-1109 (2009).
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1
  • 86
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of nemo in nf-κb activation
    • Tokunaga, F. et al. Involvement of linear polyubiquitylation of NEMO in NF-κB activation. Nature Cell Biol. 11, 123-132 (2009).
    • (2009) Nature Cell Biol , vol.11 , pp. 123-132
    • Tokunaga, F.1
  • 87
    • 84858113865 scopus 로고    scopus 로고
    • No one can whistle a symphony alone - How different ubiquitin linkages cooperate to orchestrate nf-κb activity
    • Schmukle, A. C. & Walczak, H. No one can whistle a symphony alone - how different ubiquitin linkages cooperate to orchestrate NF-κB activity. J. Cell Sci. 125, 549-559 (2012).
    • (2012) J. Cell Sci , vol.125 , pp. 549-559
    • Schmukle, A.C.1    Walczak, H.2
  • 88
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the tnf-r1 signaling complex and is required for tnf-mediated gene induction
    • Haas, T. L. et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol. Cell 36, 831-844 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 831-844
    • Haas, T.L.1
  • 89
    • 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
  • 90
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on toll-like receptors
    • Kawai, T. & Akira, S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nature Immunol. 11, 373-384 (2010).
    • (2010) Nature Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 91
    • 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. 443, 355-359 (2012).
    • (2012) Biochem. J , vol.443 , pp. 355-359
    • Kenneth, N.S.1
  • 92
    • 48749090228 scopus 로고    scopus 로고
    • Essential cytoplasmic translocation of a cytokine receptor-assembled signaling complex
    • Matsuzawa, A. et al. Essential cytoplasmic translocation of a cytokine receptor-assembled signaling complex. Science 321, 663-668 (2008).
    • (2008) Science , vol.321 , pp. 663-668
    • Matsuzawa, A.1
  • 93
    • 77952241062 scopus 로고    scopus 로고
    • Proapoptotic signalling through toll-like receptor-3 involves trif-dependent activation of caspase-8 and is under the control of inhibitor of apoptosis proteins in melanoma cells
    • Weber, A. et al. Proapoptotic signalling through Toll-like receptor-3 involves TRIF-dependent activation of caspase-8 and is under the control of inhibitor of apoptosis proteins in melanoma cells. Cell Death Differ. 17, 942-951 (2010).
    • (2010) Cell Death Differ , vol.17 , pp. 942-951
    • Weber, A.1
  • 96
    • 30544447047 scopus 로고    scopus 로고
    • Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response
    • DOI 10.1038/nature04374, PII NATURE04374
    • Oganesyan, G. et al. Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response. Nature 439, 208-211 (2006). (Pubitemid 43083142)
    • (2006) Nature , vol.439 , Issue.7073 , pp. 208-211
    • Oganesyan, G.1    Saha, S.K.2    Guo, B.3    He, J.Q.4    Shahangian, A.5    Zarnegar, B.6    Perry, A.7    Cheng, G.8
  • 99
    • 0038363463 scopus 로고    scopus 로고
    • Triggering the interferon antiviral response through an IKK-related pathway
    • DOI 10.1126/science.1081315
    • Sharma, S. et al. Triggering the interferon antiviral response through an IKK-related pathway. Science 300, 1148-1151 (2003). (Pubitemid 36583100)
    • (2003) Science , vol.300 , Issue.5622 , pp. 1148-1151
    • Sharma, S.1    TenOever, B.R.2    Grandvaux, N.3    Zhou, G.-P.4    Lin, R.5    Hiscott, J.6
  • 100
    • 61349146561 scopus 로고    scopus 로고
    • Traf6 and mekk1 play a pivotal role in the rig-i-like helicase antiviral pathway
    • Yoshida, R. et al. TRAF6 and MEKK1 play a pivotal role in the RIG-I-like helicase antiviral pathway. J. Biol. Chem. 283, 36211-36220 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 36211-36220
    • Yoshida, R.1
  • 101
    • 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
  • 102
    • 79954583057 scopus 로고    scopus 로고
    • Deletion of ciap1 and ciap2 in murine b lymphocytes constitutively activates cell survival pathways and inactivates the germinal center response
    • Gardam, S. et al. Deletion of cIAP1 and cIAP2 in murine B lymphocytes constitutively activates cell survival pathways and inactivates the germinal center response. Blood 117, 4041-4051 (2011).
    • (2011) Blood , vol.117 , pp. 4041-4051
    • Gardam, S.1
  • 103
    • 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
  • 104
    • 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
  • 105
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in nlrp3 inflammasome activation
    • Zhou, R., Yazdi, A. S., Menu, P. & Tschopp, J. A role for mitochondria in NLRP3 inflammasome activation. Nature 469, 221-225 (2011).
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 106
    • 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 137, 721-735 (2009).
    • (2009) Cell , vol.137 , pp. 721-735
    • Jin, Z.1
  • 107
    • 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
  • 108
    • 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
  • 109
    • 35948994157 scopus 로고    scopus 로고
    • Autocrine TNFα Signaling Renders Human Cancer Cells Susceptible to Smac-Mimetic-Induced Apoptosis
    • DOI 10.1016/j.ccr.2007.08.029, PII S1535610807002619
    • Petersen, S. L. et al. Autocrine TNFα signaling renders human cancer cells susceptible to Smac-mimetic-induced apoptosis. Cancer Cell 12, 445-456 (2007). (Pubitemid 350064365)
    • (2007) Cancer Cell , vol.12 , Issue.5 , pp. 445-456
    • Petersen, S.L.1    Wang, L.2    Yalcin-Chin, A.3    Li, L.4    Peyton, M.5    Minna, J.6    Harran, P.7    Wang, X.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.