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Volumn 21, Issue 11, 2014, Pages 1667-1676

TAK1 control of cell death

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; TRANSFORMING GROWTH FACTOR BETA ACTIVATED KINASE 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MAP KINASE KINASE KINASE 7; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE;

EID: 84926066792     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2014.123     Document Type: Review
Times cited : (217)

References (133)
  • 2
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl HL. Activators and target genes of Rel/NF-κB transcription factors. Oncogene 1999; 18: 6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 3
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden MS, Ghosh S. Shared principles in NF-κB signaling. Cell 2008; 132: 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 4
    • 0029551805 scopus 로고
    • Identification of a member of the MAPKKK family as a potential mediator of TGF-β signal transduction
    • Yamaguchi K, Shirakabe K, Shibuya H, Irie K, Oishi I, Ueno N et al. Identification of a member of the MAPKKK family as a potential mediator of TGF-β signal transduction. Science 1995; 270: 2008-2011.
    • (1995) Science , vol.270 , pp. 2008-2011
    • Yamaguchi, K.1    Shirakabe, K.2    Shibuya, H.3    Irie, K.4    Oishi, I.5    Ueno, N.6
  • 5
    • 84880847105 scopus 로고    scopus 로고
    • Cell type-specific function of TAK1 in innate immune signaling
    • Ajibade AA, Wang HY, Wang RF. Cell type-specific function of TAK1 in innate immune signaling. Trends Immunol 2013; 34: 307-316.
    • (2013) Trends Immunol , vol.34 , pp. 307-316
    • Ajibade, A.A.1    Wang, H.Y.2    Wang, R.F.3
  • 6
    • 0033580466 scopus 로고    scopus 로고
    • The kinase TAK1 can activate the NIK-IκB as well as the MAP kinase cascade in the IL-1 signalling pathway
    • Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K. The kinase TAK1 can activate the NIK-IκB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature 1999; 398: 252-256.
    • (1999) Nature , vol.398 , pp. 252-256
    • Ninomiya-Tsuji, J.1    Kishimoto, K.2    Hiyama, A.3    Inoue, J.4    Cao, Z.5    Matsumoto, K.6
  • 7
    • 84866731086 scopus 로고    scopus 로고
    • Targeting of TAK1 in inflammatory disorders and cancer
    • Sakurai H. Targeting of TAK1 in inflammatory disorders and cancer. Trends Pharmacol Sci 2012; 33: 522-530.
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 522-530
    • Sakurai, H.1
  • 8
    • 27544434183 scopus 로고    scopus 로고
    • Essential function for the kinase TAK1 in innate and adaptive immune responses
    • Sato S, Sanjo H, Takeda K, Ninomiya-Tsuji J, Yamamoto M, Kawai T et al. Essential function for the kinase TAK1 in innate and adaptive immune responses. Nat Immunol 2005; 6: 1087-1095.
    • (2005) Nat Immunol , vol.6 , pp. 1087-1095
    • Sato, S.1    Sanjo, H.2    Takeda, K.3    Ninomiya-Tsuji, J.4    Yamamoto, M.5    Kawai, T.6
  • 9
    • 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 PH, Matsuzawa A, Zhang W, Mino T, Vignali DA, Karin M. Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines. Nat Immunol 2010; 11: 70-75.
    • (2010) Nat Immunol , vol.11 , pp. 70-75
    • Tseng, P.H.1    Matsuzawa, A.2    Zhang, W.3    Mino, T.4    Vignali, D.A.5    Karin, M.6
  • 10
    • 33748999526 scopus 로고    scopus 로고
    • TAK1 is indispensable for development of T cells and prevention of colitis by the generation of regulatory T cells
    • Sato S, Sanjo H, Tsujimura T, Ninomiya-Tsuji J, Yamamoto M, Kawai T et al. TAK1 is indispensable for development of T cells and prevention of colitis by the generation of regulatory T cells. Int Immunol 2006; 18: 1405-1411.
    • (2006) Int Immunol , vol.18 , pp. 1405-1411
    • Sato, S.1    Sanjo, H.2    Tsujimura, T.3    Ninomiya-Tsuji, J.4    Yamamoto, M.5    Kawai, T.6
  • 11
    • 33746111852 scopus 로고    scopus 로고
    • The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function
    • Wan YY, Chi H, Xie M, Schneider MD, Flavell RA. The kinase TAK1 integrates antigen and cytokine receptor signaling for T cell development, survival and function. Nat Immunol 2006; 7: 851-858.
    • (2006) Nat Immunol , vol.7 , pp. 851-858
    • Wan, Y.Y.1    Chi, H.2    Xie, M.3    Schneider, M.D.4    Flavell, R.A.5
  • 12
    • 33746857795 scopus 로고    scopus 로고
    • Essential role of TAK1 in thymocyte development and activation
    • Liu HH, Xie M, Schneider MD, Chen ZJ. Essential role of TAK1 in thymocyte development and activation. Proc Natl Acad Sci USA 2006; 103: 11677-11682.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11677-11682
    • Liu, H.H.1    Xie, M.2    Schneider, M.D.3    Chen, Z.J.4
  • 13
    • 0030968634 scopus 로고    scopus 로고
    • TAK1 mediates the ceramide signaling to stress-activated protein kinase/c-Jun N-terminal kinase
    • Shirakabe K, Yamaguchi K, Shibuya H, Irie K, Matsuda S, Moriguchi T et al. TAK1 mediates the ceramide signaling to stress-activated protein kinase/c-Jun N-terminal kinase. J Biol Chem 1997; 272: 8141-8144.
    • (1997) J Biol Chem , vol.272 , pp. 8141-8144
    • Shirakabe, K.1    Yamaguchi, K.2    Shibuya, H.3    Irie, K.4    Matsuda, S.5    Moriguchi, T.6
  • 16
    • 57749122042 scopus 로고    scopus 로고
    • TAK1-binding protein 1, TAB1, mediates osmotic stress-induced TAK1 activation but is dispensable for TAK1-mediated cytokine signaling
    • Inagaki M, Omori E, Kim JY, Komatsu Y, Scott G, Ray MK et al. TAK1-binding protein 1, TAB1, mediates osmotic stress-induced TAK1 activation but is dispensable for TAK1-mediated cytokine signaling. J Biol Chem 2008; 283: 33080-33086.
    • (2008) J Biol Chem , vol.283 , pp. 33080-33086
    • Inagaki, M.1    Omori, E.2    Kim, J.Y.3    Komatsu, Y.4    Scott, G.5    Ray, M.K.6
  • 17
    • 33751229931 scopus 로고    scopus 로고
    • A pivotal role for endogenous TGF-β-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway
    • Xie M, Zhang D, Dyck JR, Li Y, Zhang H, Morishima M et al. A pivotal role for endogenous TGF-β-activated kinase-1 in the LKB1/AMP-activated protein kinase energy-sensor pathway. Proc Natl Acad Sci USA 2006; 103: 17378-17383.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17378-17383
    • Xie, M.1    Zhang, D.2    Dyck, J.R.3    Li, Y.4    Zhang, H.5    Morishima, M.6
  • 18
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ. Activation of IKK by TNFα requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 2006; 22: 245-257.
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 21
    • 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 TL, Emmerich CH, Gerlach B, Schmukle AC, Cordier SM, Rieser E 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 2009; 36: 831-844.
    • (2009) Mol Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6
  • 23
    • 17844393079 scopus 로고    scopus 로고
    • TAK1-binding protein 2 facilitates ubiquitination of TRAF6 and assembly of TRAF6 with IKK in the IL-1 signaling pathway
    • Kishida S, Sanjo H, Akira S, Matsumoto K, Ninomiya-Tsuji J. TAK1-binding protein 2 facilitates ubiquitination of TRAF6 and assembly of TRAF6 with IKK in the IL-1 signaling pathway. Genes Cells 2005; 10: 447-454.
    • (2005) Genes Cells , vol.10 , pp. 447-454
    • Kishida, S.1    Sanjo, H.2    Akira, S.3    Matsumoto, K.4    Ninomiya-Tsuji, J.5
  • 24
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TAB3 activate the NF-κB pathway through binding to polyubiquitin chains
    • Kanayama A, Seth RB, Sun L, Ea CK, Hong M, Shaito A et al. TAB2 and TAB3 activate the NF-κB pathway through binding to polyubiquitin chains. Mol Cell 2004; 15: 535-548.
    • (2004) Mol Cell , vol.15 , pp. 535-548
    • Kanayama, A.1    Seth, R.B.2    Sun, L.3    Ea, C.K.4    Hong, M.5    Shaito, A.6
  • 25
    • 27744577296 scopus 로고    scopus 로고
    • TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
    • Shim JH, Xiao C, Paschal AE, Bailey ST, Rao P, Hayden MS et al. TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo. Genes Dev 2005; 19: 2668-2681.
    • (2005) Genes Dev , vol.19 , pp. 2668-2681
    • Shim, J.H.1    Xiao, C.2    Paschal, A.E.3    Bailey, S.T.4    Rao, P.5    Hayden, M.S.6
  • 26
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNFα-induced cell death by inducing c-FLIP(L) turnover
    • Chang L, Kamata H, Solinas G, Luo JL, Maeda S, Venuprasad K et al. The E3 ubiquitin ligase itch couples JNK activation to TNFα-induced cell death by inducing c-FLIP(L) turnover. Cell 2006; 124: 601-613.
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1    Kamata, H.2    Solinas, G.3    Luo, J.L.4    Maeda, S.5    Venuprasad, K.6
  • 27
    • 0032508414 scopus 로고    scopus 로고
    • NF-κB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang CY, Mayo MW, Korneluk RG, Goeddel DV, Baldwin AS Jr. NF-κB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 1998; 281: 1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin, A.S.5
  • 28
    • 33748747706 scopus 로고    scopus 로고
    • Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro
    • Momcilovic M, Hong SP, Carlson M. Mammalian TAK1 activates Snf1 protein kinase in yeast and phosphorylates AMP-activated protein kinase in vitro. J Biol Chem 2006; 281: 25336-25343.
    • (2006) J Biol Chem , vol.281 , pp. 25336-25343
    • Momcilovic, M.1    Hong, S.P.2    Carlson, M.3
  • 31
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu G, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, Irie K et al. TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol Cell 2000; 5: 649-658.
    • (2000) Mol Cell , vol.5 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6
  • 33
    • 77955497476 scopus 로고    scopus 로고
    • Autoactivation of transforming growth factor β-activated kinase 1 is a sequential bimolecular process
    • Scholz R, Sidler CL, Thali RF, Winssinger N, Cheung PC, Neumann D. Autoactivation of transforming growth factor β-activated kinase 1 is a sequential bimolecular process. J Biol Chem 2010; 285: 25753-25766.
    • (2010) J Biol Chem , vol.285 , pp. 25753-25766
    • Scholz, R.1    Sidler, C.L.2    Thali, R.F.3    Winssinger, N.4    Cheung, P.C.5    Neumann, D.6
  • 34
    • 0034629146 scopus 로고    scopus 로고
    • TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop
    • Kishimoto K, Matsumoto K, Ninomiya-Tsuji J. TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop. J Biol Chem 2000; 275: 7359-7364.
    • (2000) J Biol Chem , vol.275 , pp. 7359-7364
    • Kishimoto, K.1    Matsumoto, K.2    Ninomiya-Tsuji, J.3
  • 36
    • 84894628175 scopus 로고    scopus 로고
    • TAK1 binding protein 2 is essential for liver protection from stressors
    • Ikeda Y, Morioka S, Matsumoto K, Ninomiya-Tsuji J. TAK1 binding protein 2 is essential for liver protection from stressors. PLoS One 2014; 9: e88037.
    • (2014) PLoS One , vol.9 , pp. e88037
    • Ikeda, Y.1    Morioka, S.2    Matsumoto, K.3    Ninomiya-Tsuji, J.4
  • 37
    • 84868609110 scopus 로고    scopus 로고
    • TAK1 kinase signaling regulates embryonic angiogenesis by modulating endothelial cell survival and migration
    • Morioka S, Inagaki M, Komatsu Y, Mishina Y, Matsumoto K, Ninomiya-Tsuji J. TAK1 kinase signaling regulates embryonic angiogenesis by modulating endothelial cell survival and migration. Blood 2012; 120: 3846-3857.
    • (2012) Blood , vol.120 , pp. 3846-3857
    • Morioka, S.1    Inagaki, M.2    Komatsu, Y.3    Mishina, Y.4    Matsumoto, K.5    Ninomiya-Tsuji, J.6
  • 38
    • 77449125293 scopus 로고    scopus 로고
    • Transforming growth factor β-activated kinase 1 (TAK1) kinase adaptor, TAK1-binding protein 2, plays dual roles in TAK1 signaling by recruiting both an activator and an inhibitor of TAK1 kinase in tumor necrosis factor signaling pathway
    • Broglie P, Matsumoto K, Akira S, Brautigan DL, Ninomiya-Tsuji J. Transforming growth factor β-activated kinase 1 (TAK1) kinase adaptor, TAK1-binding protein 2, plays dual roles in TAK1 signaling by recruiting both an activator and an inhibitor of TAK1 kinase in tumor necrosis factor signaling pathway. J Biol Chem 2010; 285: 2333-2339.
    • (2010) J Biol Chem , vol.285 , pp. 2333-2339
    • Broglie, P.1    Matsumoto, K.2    Akira, S.3    Brautigan, D.L.4    Ninomiya-Tsuji, J.5
  • 39
    • 33845994781 scopus 로고    scopus 로고
    • Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway
    • Kajino T, Ren H, Iemura S, Natsume T, Stefansson B, Brautigan DL et al. Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway. J Biol Chem 2006; 281: 39891-39896.
    • (2006) J Biol Chem , vol.281 , pp. 39891-39896
    • Kajino, T.1    Ren, H.2    Iemura, S.3    Natsume, T.4    Stefansson, B.5    Brautigan, D.L.6
  • 40
    • 44849108079 scopus 로고    scopus 로고
    • Protein phosphatase 2A is a negative regulator of transforming growth factor-β1-induced TAK1 activation in mesangial cells
    • Kim SI, Kwak JH, Wang L, Choi ME. Protein phosphatase 2A is a negative regulator of transforming growth factor-β1-induced TAK1 activation in mesangial cells. J Biol Chem 2008; 283: 10753-10763.
    • (2008) J Biol Chem , vol.283 , pp. 10753-10763
    • Kim, S.I.1    Kwak, J.H.2    Wang, L.3    Choi, M.E.4
  • 41
    • 84857775368 scopus 로고    scopus 로고
    • Epithelial transforming growth factor β-activated kinase 1 (TAK1) is activated through two independent mechanisms and regulates reactive oxygen species
    • Omori E, Inagaki M, Mishina Y, Matsumoto K, Ninomiya-Tsuji J. Epithelial transforming growth factor β-activated kinase 1 (TAK1) is activated through two independent mechanisms and regulates reactive oxygen species. Proc Natl Acad Sci USA 2012; 109: 3365-3370.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 3365-3370
    • Omori, E.1    Inagaki, M.2    Mishina, Y.3    Matsumoto, K.4    Ninomiya-Tsuji, J.5
  • 42
    • 84899697653 scopus 로고    scopus 로고
    • Activated macrophage survival is coordinated by TAK1 binding proteins
    • Mihaly SR, Morioka S, Ninomiya-Tsuji J, Takaesu G. Activated macrophage survival is coordinated by TAK1 binding proteins. PLoS One 2014; 9: e94982.
    • (2014) PLoS One , vol.9 , pp. e94982
    • Mihaly, S.R.1    Morioka, S.2    Ninomiya-Tsuji, J.3    Takaesu, G.4
  • 43
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003; 114: 181-190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 46
    • 84874263775 scopus 로고    scopus 로고
    • Necroptosis: The release of damageassociated molecular patterns and its physiological relevance
    • Kaczmarek A, Vandenabeele P, Krysko DV. Necroptosis: the release of damageassociated molecular patterns and its physiological relevance. Immunity 2013; 38: 209-223.
    • (2013) Immunity , vol.38 , pp. 209-223
    • Kaczmarek, A.1    Vandenabeele, P.2    Krysko, D.V.3
  • 48
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α. Cell 2009; 137: 1100-1111.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6
  • 49
    • 84894024528 scopus 로고    scopus 로고
    • TAK1 kinase switches cell fate from apoptosis to necrosis following TNF stimulation
    • Morioka S, Broglie P, Omori E, Ikeda Y, Takaesu G, Matsumoto K et al. TAK1 kinase switches cell fate from apoptosis to necrosis following TNF stimulation. J Cell Biol 2014; 204: 607-623.
    • (2014) J Cell Biol , vol.204 , pp. 607-623
    • Morioka, S.1    Broglie, P.2    Omori, E.3    Ikeda, Y.4    Takaesu, G.5    Matsumoto, K.6
  • 50
    • 0032522738 scopus 로고    scopus 로고
    • IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases
    • Deveraux QL, Roy N, Stennicke HR, Van Arsdale T, Zhou Q, Srinivasula SM et al. IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. EMBO J 1998; 17: 2215-2223.
    • (1998) EMBO J , vol.17 , pp. 2215-2223
    • Deveraux, Q.L.1    Roy, N.2    Stennicke, H.R.3    Van Arsdale, T.4    Zhou, Q.5    Srinivasula, S.M.6
  • 51
    • 80054888589 scopus 로고    scopus 로고
    • It cuts both ways: Reconciling the dual roles of caspase 8 in cell death and survival
    • Oberst A, Green DR. It cuts both ways: reconciling the dual roles of caspase 8 in cell death and survival. Nat Rev Mol Cell Biol 2011; 12: 757-763.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 757-763
    • Oberst, A.1    Green, D.R.2
  • 53
    • 0037099678 scopus 로고    scopus 로고
    • C-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis
    • Chang DW, Xing Z, Pan Y, Algeciras-Schimnich A, Barnhart BC, Yaish-Ohad S et al. c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. EMBO J 2002; 21: 3704-3714.
    • (2002) EMBO J , vol.21 , pp. 3704-3714
    • Chang, D.W.1    Xing, Z.2    Pan, Y.3    Algeciras-Schimnich, A.4    Barnhart, B.C.5    Yaish-Ohad, S.6
  • 54
    • 79952810024 scopus 로고    scopus 로고
    • Catalytic activity of the caspase-8-FLIP(L) complex inhibits RIPK3-dependent necrosis
    • Oberst A, Dillon CP, Weinlich R, McCormick LL, Fitzgerald P, Pop C 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    Dillon, C.P.2    Weinlich, R.3    McCormick, L.L.4    Fitzgerald, P.5    Pop, C.6
  • 55
    • 49049095991 scopus 로고    scopus 로고
    • Enterocyte-derived TAK1 signaling prevents epithelium apoptosis and the development of ileitis and colitis
    • Kajino-Sakamoto R, Inagaki M, Lippert E, Akira S, Robine S, Matsumoto K et al. Enterocyte-derived TAK1 signaling prevents epithelium apoptosis and the development of ileitis and colitis. J Immunol 2008; 181: 1143-1152.
    • (2008) J Immunol , vol.181 , pp. 1143-1152
    • Kajino-Sakamoto, R.1    Inagaki, M.2    Lippert, E.3    Akira, S.4    Robine, S.5    Matsumoto, K.6
  • 56
    • 34047173496 scopus 로고    scopus 로고
    • Epithelial NEMO links innate immunity to chronic intestinal inflammation
    • Nenci A, Becker C, Wullaert A, Gareus R, van Loo G, Danese S et al. Epithelial NEMO links innate immunity to chronic intestinal inflammation. Nature 2007; 446: 557-561.
    • (2007) Nature , vol.446 , pp. 557-561
    • Nenci, A.1    Becker, C.2    Wullaert, A.3    Gareus, R.4    Van Loo, G.5    Danese, S.6
  • 57
    • 77952107213 scopus 로고    scopus 로고
    • TAK1 suppresses a NEMO-dependent but NF-κB-independent pathway to liver cancer
    • Bettermann K, Vucur M, Haybaeck J, Koppe C, Janssen J, Heymann F et al. TAK1 suppresses a NEMO-dependent but NF-κB-independent pathway to liver cancer. Cancer Cell 2010; 17: 481-496.
    • (2010) Cancer Cell , vol.17 , pp. 481-496
    • Bettermann, K.1    Vucur, M.2    Haybaeck, J.3    Koppe, C.4    Janssen, J.5    Heymann, F.6
  • 58
    • 84873033324 scopus 로고    scopus 로고
    • TAK1 is essential for osteoclast differentiation and is an important modulator of cell death by apoptosis and necroptosis
    • Lamothe B, Lai Y, Xie M, Schneider MD, Darnay BG. TAK1 is essential for osteoclast differentiation and is an important modulator of cell death by apoptosis and necroptosis. Mol Cell Biol 2013; 33: 582-595.
    • (2013) Mol Cell Biol , vol.33 , pp. 582-595
    • Lamothe, B.1    Lai, Y.2    Xie, M.3    Schneider, M.D.4    Darnay, B.G.5
  • 59
    • 80053927315 scopus 로고    scopus 로고
    • The prevalence of TNFα-induced necrosis over apoptosis is determined by TAK1-RIP1 interplay
    • Arslan SC, Scheidereit C. The prevalence of TNFα-induced necrosis over apoptosis is determined by TAK1-RIP1 interplay. PLoS One 2011; 6: e26069.
    • (2011) PLoS One , vol.6 , pp. e26069
    • Arslan, S.C.1    Scheidereit, C.2
  • 60
    • 0029858348 scopus 로고    scopus 로고
    • RIP mediates tumor necrosis factor receptor 1 activation of NF-κB but not Fas/APO-1-initiated apoptosis
    • Ting AT, Pimentel-Muinos FX, Seed B. RIP mediates tumor necrosis factor receptor 1 activation of NF-κB but not Fas/APO-1-initiated apoptosis. EMBO J 1996; 15: 6189-6196.
    • (1996) EMBO J , vol.15 , pp. 6189-6196
    • Ting, A.T.1    Pimentel-Muinos, F.X.2    Seed, B.3
  • 61
    • 84886305117 scopus 로고    scopus 로고
    • Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death
    • Ofengeim D, Yuan J. Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death. Nat Rev Mol Cell Biol 2013; 14: 727-736.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 727-736
    • Ofengeim, D.1    Yuan, J.2
  • 62
    • 43049152912 scopus 로고    scopus 로고
    • TNF-α induces two distinct caspase-8 activation pathways
    • Wang L, Du F, Wang X. TNF-α induces two distinct caspase-8 activation pathways. Cell 2008; 133: 693-703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 63
    • 79960921946 scopus 로고    scopus 로고
    • The ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • Tenev T, Bianchi K, Darding M, Broemer M, Langlais C, Wallberg F 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    Bianchi, K.2    Darding, M.3    Broemer, M.4    Langlais, C.5    Wallberg, F.6
  • 64
    • 44949240664 scopus 로고    scopus 로고
    • CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell 2008; 30: 689-700.
    • (2008) Mol Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.1    Milutinovic, S.2    Dickson, K.M.3    Ho, W.C.4    Boudreault, A.5    Durkin, J.6
  • 65
    • 78049504143 scopus 로고    scopus 로고
    • TGF-β-activated kinase 1 signaling maintains intestinal integrity by preventing accumulation of reactive oxygen species in the intestinal epithelium
    • Kajino-Sakamoto R, Omori E, Nighot PK, Blikslager AT, Matsumoto K, Ninomiya-Tsuji J. TGF-β-activated kinase 1 signaling maintains intestinal integrity by preventing accumulation of reactive oxygen species in the intestinal epithelium. J Immunol 2010; 185: 4729-4737.
    • (2010) J Immunol , vol.185 , pp. 4729-4737
    • Kajino-Sakamoto, R.1    Omori, E.2    Nighot, P.K.3    Blikslager, A.T.4    Matsumoto, K.5    Ninomiya-Tsuji, J.6
  • 66
    • 54449085568 scopus 로고    scopus 로고
    • TAK1 regulates reactive oxygen species and cell death in keratinocytes, which is essential for skin integrity
    • Omori E, Morioka S, Matsumoto K, Ninomiya-Tsuji J. TAK1 regulates reactive oxygen species and cell death in keratinocytes, which is essential for skin integrity. J Biol Chem 2008; 283: 26161-26168.
    • (2008) J Biol Chem , vol.283 , pp. 26161-26168
    • Omori, E.1    Morioka, S.2    Matsumoto, K.3    Ninomiya-Tsuji, J.4
  • 67
    • 84898027331 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3
    • Wang H, Sun L, Su L, Rizo J, Liu L, Wang LF et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol Cell 2014; 54: 133-146.
    • (2014) Mol Cell , vol.54 , pp. 133-146
    • Wang, H.1    Sun, L.2    Su, L.3    Rizo, J.4    Liu, L.5    Wang, L.F.6
  • 68
    • 84893325471 scopus 로고    scopus 로고
    • Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
    • Cai Z, Jitkaew S, Zhao J, Chiang HC, Choksi S, Liu J et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat Cell Biol 2014; 16: 55-65.
    • (2014) Nat Cell Biol , vol.16 , pp. 55-65
    • Cai, Z.1    Jitkaew, S.2    Zhao, J.3    Chiang, H.C.4    Choksi, S.5    Liu, J.6
  • 69
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • Sun L, Wang H, Wang Z, He S, Chen S, Liao D et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 2012; 148: 213-227.
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1    Wang, H.2    Wang, Z.3    He, S.4    Chen, S.5    Liao, D.6
  • 70
    • 84862909353 scopus 로고    scopus 로고
    • The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways
    • Wang Z, Jiang H, Chen S, Du F, Wang X. The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways. Cell 2012; 148: 228-243.
    • (2012) Cell , vol.148 , pp. 228-243
    • Wang, Z.1    Jiang, H.2    Chen, S.3    Du, F.4    Wang, X.5
  • 71
    • 84901257054 scopus 로고    scopus 로고
    • Depletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis
    • Remijsen Q, Goossens V, Grootjans S, Van den Haute C, Vanlangenakker N, Dondelinger Y et al. Depletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis. Cell Death Dis 2014; 5: e1004.
    • (2014) Cell Death Dis , vol.5 , pp. e1004
    • Remijsen, Q.1    Goossens, V.2    Grootjans, S.3    Van Den-Haute, C.4    Vanlangenakker, N.5    Dondelinger, Y.6
  • 73
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M 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    Challa, S.2    Moquin, D.3    Genga, R.4    Ray, T.D.5    Guildford, M.6
  • 74
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α. Cell 2009; 137: 1100-1111.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6
  • 75
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang DW, Shao J, Lin J, Zhang N, Lu BJ, Lin SC et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 2009; 325: 332-336.
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1    Shao, J.2    Lin, J.3    Zhang, N.4    Lu, B.J.5    Lin, S.C.6
  • 77
    • 80053927315 scopus 로고    scopus 로고
    • The prevalence of TNFα-induced necrosis over apoptosis is determined by TAK1-RIP1 interplay
    • Arslan SC, Scheidereit C. The prevalence of TNFα-induced necrosis over apoptosis is determined by TAK1-RIP1 interplay. PLoS One 2011; 6: e26069.
    • (2011) PLoS One , vol.6 , pp. e26069
    • Arslan, S.C.1    Scheidereit, C.2
  • 78
    • 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, Vanden Berghe T, Bogaert P, Laukens B, Zobel K, Deshayes K et al. cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production. Cell Death Differ 2011; 18: 656-665.
    • (2011) Cell Death Differ , vol.18 , pp. 656-665
    • Vanlangenakker, N.1    Vanden Berghe, T.2    Bogaert, P.3    Laukens, B.4    Zobel, K.5    Deshayes, K.6
  • 79
    • 84883770753 scopus 로고    scopus 로고
    • RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition
    • Dondelinger Y, Aguileta MA, Goossens V, Dubuisson C, Grootjans S, Dejardin E et al. RIPK3 contributes to TNFR1-mediated RIPK1 kinase-dependent apoptosis in conditions of cIAP1/2 depletion or TAK1 kinase inhibition. Cell Death Differ 2013; 20: 1381-1392.
    • (2013) Cell Death Differ , vol.20 , pp. 1381-1392
    • Dondelinger, Y.1    Aguileta, M.A.2    Goossens, V.3    Dubuisson, C.4    Grootjans, S.5    Dejardin, E.6
  • 81
    • 84901422731 scopus 로고    scopus 로고
    • RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis
    • Rickard JA, O'Donnell JA, Evans JM, Lalaoui N, Poh AR, Rogers T et al. RIPK1 regulates RIPK3-MLKL-driven systemic inflammation and emergency hematopoiesis. Cell 2014; 157: 1175-1188.
    • (2014) Cell , vol.157 , pp. 1175-1188
    • Rickard, J.A.1    O'Donnell, J.A.2    Evans, J.M.3    Lalaoui, N.4    Poh, A.R.5    Rogers, T.6
  • 82
    • 33745851830 scopus 로고    scopus 로고
    • TAK1 is a master regulator of epidermal homeostasis involving skin inflammation and apoptosis
    • Omori E, Matsumoto K, Sanjo H, Sato S, Akira S, Smart RC et al. TAK1 is a master regulator of epidermal homeostasis involving skin inflammation and apoptosis. J Biol Chem 2006; 281: 19610-19617.
    • (2006) J Biol Chem , vol.281 , pp. 19610-19617
    • Omori, E.1    Matsumoto, K.2    Sanjo, H.3    Sato, S.4    Akira, S.5    Smart, R.C.6
  • 83
    • 76249087046 scopus 로고    scopus 로고
    • Disruption of TAK1 in hepatocytes causes hepatic injury, inflammation, fibrosis, and carcinogenesis
    • Inokuchi S, Aoyama T, Miura K, Osterreicher CH, Kodama Y, Miyai K et al. Disruption of TAK1 in hepatocytes causes hepatic injury, inflammation, fibrosis, and carcinogenesis. Proc Natl Acad Sci USA 2010; 107: 844-849.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 844-849
    • Inokuchi, S.1    Aoyama, T.2    Miura, K.3    Osterreicher, C.H.4    Kodama, Y.5    Miyai, K.6
  • 84
    • 84870712635 scopus 로고    scopus 로고
    • TAK1 (MAP3K7) signaling regulates hematopoietic stem cells through TNF-dependent and -independent mechanisms
    • Takaesu G, Inagaki M, Takubo K, Mishina Y, Hess PR, Dean GA et al. TAK1 (MAP3K7) signaling regulates hematopoietic stem cells through TNF-dependent and -independent mechanisms. PLoS One 2012; 7: e51073.
    • (2012) PLoS One , vol.7 , pp. e51073
    • Takaesu, G.1    Inagaki, M.2    Takubo, K.3    Mishina, Y.4    Hess, P.R.5    Dean, G.A.6
  • 85
    • 82955189314 scopus 로고    scopus 로고
    • TNF-α/Fas-RIP-1-induced cell death signaling separates murine hematopoietic stem cells/progenitors into 2 distinct populations
    • Xiao Y, Li H, Zhang J, Volk A, Zhang S, Wei W et al. TNF-α/Fas-RIP-1-induced cell death signaling separates murine hematopoietic stem cells/progenitors into 2 distinct populations. Blood 2011; 118: 6057-6067.
    • (2011) Blood , vol.118 , pp. 6057-6067
    • Xiao, Y.1    Li, H.2    Zhang, J.3    Volk, A.4    Zhang, S.5    Wei, W.6
  • 86
    • 46949097612 scopus 로고    scopus 로고
    • TAK1 is required for the survival of hematopoietic cells and hepatocytes in mice
    • Tang M, Wei X, Guo Y, Breslin P, Zhang S, Zhang S et al. TAK1 is required for the survival of hematopoietic cells and hepatocytes in mice. J Exp Med 2008; 205: 1611-1619.
    • (2008) J Exp Med , vol.205 , pp. 1611-1619
    • Tang, M.1    Wei, X.2    Guo, Y.3    Breslin, P.4    Zhang, S.5    Zhang, S.6
  • 87
    • 84856301921 scopus 로고    scopus 로고
    • TAK1 negatively regulates NF-κB and p38 MAP kinase activation in Gr-1+CD11b+ neutrophils
    • Ajibade AA, Wang Q, Cui J, Zou J, Xia X, Wang M et al. TAK1 negatively regulates NF-κB and p38 MAP kinase activation in Gr-1+CD11b+ neutrophils. Immunity 2012; 36: 43-54.
    • (2012) Immunity , vol.36 , pp. 43-54
    • Ajibade, A.A.1    Wang, Q.2    Cui, J.3    Zou, J.4    Xia, X.5    Wang, M.6
  • 88
    • 84883296695 scopus 로고    scopus 로고
    • RIP3 inhibits inflammatory hepatocarcinogenesis but promotes cholestasis by controlling caspase-8- and JNK-dependent compensatory cell proliferation
    • Vucur M, Reisinger F, Gautheron J, Janssen J, Roderburg C, Cardenas DV et al. RIP3 inhibits inflammatory hepatocarcinogenesis but promotes cholestasis by controlling caspase-8- and JNK-dependent compensatory cell proliferation. Cell Rep 2013; 4: 776-790.
    • (2013) Cell Rep , vol.4 , pp. 776-790
    • Vucur, M.1    Reisinger, F.2    Gautheron, J.3    Janssen, J.4    Roderburg, C.5    Cardenas, D.V.6
  • 89
    • 84870922929 scopus 로고    scopus 로고
    • Deletion of TAK1 in the myeloid lineage results in the spontaneous development of myelomonocytic leukemia in mice
    • Lamothe B, Lai Y, Hur L, Orozco NM, Wang J, Campos AD et al. Deletion of TAK1 in the myeloid lineage results in the spontaneous development of myelomonocytic leukemia in mice. PLoS One 2012; 7: e51228.
    • (2012) PLoS One , vol.7 , pp. e51228
    • Lamothe, B.1    Lai, Y.2    Hur, L.3    Orozco, N.M.4    Wang, J.5    Campos, A.D.6
  • 91
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev A, Huang Z, Boyce M, Li Y, Jagtap P, Mizushima N et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat Chem Biol 2005; 1: 112-119.
    • (2005) Nat Chem Biol , vol.1 , pp. 112-119
    • Degterev, A.1    Huang, Z.2    Boyce, M.3    Li, Y.4    Jagtap, P.5    Mizushima, N.6
  • 92
  • 93
    • 80052845560 scopus 로고    scopus 로고
    • Caspase-8 regulates TNF-α-induced epithelial necroptosis and terminal ileitis
    • Gunther C, Martini E, Wittkopf N, Amann K, Weigmann B, Neumann H 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
    • Gunther, C.1    Martini, E.2    Wittkopf, N.3    Amann, K.4    Weigmann, B.5    Neumann, H.6
  • 94
    • 80755132824 scopus 로고    scopus 로고
    • The adaptor protein FADD protects epidermal keratinocytes from necroptosis in vivo and prevents skin inflammation
    • Bonnet MC, Preukschat D, Welz PS, van Loo G, Ermolaeva MA, Bloch W 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    Preukschat, D.2    Welz, P.S.3    Van Loo, G.4    Ermolaeva, M.A.5    Bloch, W.6
  • 95
    • 80052850704 scopus 로고    scopus 로고
    • FADD prevents RIP3-mediated epithelial cell necrosis and chronic intestinal inflammation
    • Welz PS, Wullaert A, Vlantis K, Kondylis V, Fernandez-Majada V, Ermolaeva M 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    Wullaert, A.2    Vlantis, K.3    Kondylis, V.4    Fernandez-Majada, V.5    Ermolaeva, M.6
  • 97
    • 84897088275 scopus 로고    scopus 로고
    • Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis
    • Newton K, Dugger DL, Wickliffe KE, Kapoor N, de Almagro MC, Vucic D et al. Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis. Science 2014; 343: 1357-1360.
    • (2014) Science , vol.343 , pp. 1357-1360
    • Newton, K.1    Dugger, D.L.2    Wickliffe, K.E.3    Kapoor, N.4    De Almagro, M.C.5    Vucic, D.6
  • 99
    • 80053580530 scopus 로고    scopus 로고
    • RIPK-dependent necrosis and its regulation by caspases: A mystery in five acts
    • Green DR, Oberst A, Dillon CP, Weinlich R, Salvesen GS. 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    Oberst, A.2    Dillon, C.P.3    Weinlich, R.4    Salvesen, G.S.5
  • 100
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin Y, Devin A, Rodriguez Y, Liu ZG. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev 1999; 13: 2514-2526.
    • (1999) Genes Dev , vol.13 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 101
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • Feng S, Yang Y, Mei Y, Ma L, Zhu DE, Hoti N 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    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.E.5    Hoti, N.6
  • 102
    • 0037903145 scopus 로고    scopus 로고
    • A resorcylic acid lactone, 5Z-7-oxozeaenol, prevents inflammation by inhibiting the catalytic activity of TAK1 MAPK kinase kinase
    • Ninomiya-Tsuji J, Kajino T, Ono K, Ohtomo T, Matsumoto M, Shiina M et al. A resorcylic acid lactone, 5Z-7-oxozeaenol, prevents inflammation by inhibiting the catalytic activity of TAK1 MAPK kinase kinase. J Biol Chem 2003; 278: 18485-18490.
    • (2003) J Biol Chem , vol.278 , pp. 18485-18490
    • Ninomiya-Tsuji, J.1    Kajino, T.2    Ono, K.3    Ohtomo, T.4    Matsumoto, M.5    Shiina, M.6
  • 103
    • 84863419728 scopus 로고    scopus 로고
    • TAK1 inhibition promotes apoptosis in KRAS-dependent colon cancers
    • Singh A, Sweeney MF, Yu M, Burger A, Greninger P, Benes C et al. TAK1 inhibition promotes apoptosis in KRAS-dependent colon cancers. Cell 2012; 148: 639-650.
    • (2012) Cell , vol.148 , pp. 639-650
    • Singh, A.1    Sweeney, M.F.2    Yu, M.3    Burger, A.4    Greninger, P.5    Benes, C.6
  • 104
    • 78449312054 scopus 로고    scopus 로고
    • Ablation of TAK1 upregulates reactive oxygen species and selectively kills tumor cells
    • Omori E, Matsumoto K, Zhu S, Smart RC, Ninomiya-Tsuji J. Ablation of TAK1 upregulates reactive oxygen species and selectively kills tumor cells. Cancer Res 2010; 70: 8417-8425.
    • (2010) Cancer Res , vol.70 , pp. 8417-8425
    • Omori, E.1    Matsumoto, K.2    Zhu, S.3    Smart, R.C.4    Ninomiya-Tsuji, J.5
  • 105
    • 0842304221 scopus 로고    scopus 로고
    • Kinase RIP3 is dispensable for normal NF-κBs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4
    • Newton K, Sun X, Dixit VM. Kinase RIP3 is dispensable for normal NF-κBs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4. Mol Cell Biol 2004; 24: 1464-1469.
    • (2004) Mol Cell Biol , vol.24 , pp. 1464-1469
    • Newton, K.1    Sun, X.2    Dixit, V.M.3
  • 106
    • 0033119952 scopus 로고    scopus 로고
    • Embryonic lethality, liver degeneration, and impaired NF-κB activation in IKK-β-deficient mice
    • Tanaka M, Fuentes ME, Yamaguchi K, Durnin MH, Dalrymple SA, Hardy KL et al. Embryonic lethality, liver degeneration, and impaired NF-κB activation in IKK-β-deficient mice. Immunity 1999; 10: 421-429.
    • (1999) Immunity , vol.10 , pp. 421-429
    • Tanaka, M.1    Fuentes, M.E.2    Yamaguchi, K.3    Durnin, M.H.4    Dalrymple, S.A.5    Hardy, K.L.6
  • 107
    • 0033532386 scopus 로고    scopus 로고
    • The IKKβ subunit of IκB kinase (IKK) is essential for nuclear factor κb activation and prevention of apoptosis
    • Li ZW, Chu W, Hu Y, Delhase M, Deerinck T, Ellisman M et al. The IKKβ subunit of IκB kinase (IKK) is essential for nuclear factor κB activation and prevention of apoptosis. J Exp Med 1999; 189: 1839-1845.
    • (1999) J Exp Med , vol.189 , pp. 1839-1845
    • Li, Z.W.1    Chu, W.2    Hu, Y.3    Delhase, M.4    Deerinck, T.5    Ellisman, M.6
  • 108
    • 0033537739 scopus 로고    scopus 로고
    • Severe liver degeneration in mice lacking the IκB kinase 2 gene
    • Li Q, Van Antwerp D, Mercurio F, Lee KF, Verma IM. Severe liver degeneration in mice lacking the IκB kinase 2 gene. Science 1999; 284: 321-325.
    • (1999) Science , vol.284 , pp. 321-325
    • Li, Q.1    Van Antwerp, D.2    Mercurio, F.3    Lee, K.F.4    Verma, I.M.5
  • 109
    • 0037142027 scopus 로고    scopus 로고
    • TNF-mediated inflammatory skin disease in mice with epidermis-specific deletion of IKK2
    • Pasparakis M, Courtois G, Hafner M, Schmidt-Supprian M, Nenci A, Toksoy A et al. TNF-mediated inflammatory skin disease in mice with epidermis-specific deletion of IKK2. Nature 2002; 417: 861-866.
    • (2002) Nature , vol.417 , pp. 861-866
    • Pasparakis, M.1    Courtois, G.2    Hafner, M.3    Schmidt-Supprian, M.4    Nenci, A.5    Toksoy, A.6
  • 110
    • 1442306054 scopus 로고    scopus 로고
    • IκB-kinaseβdependent NF-κB activation provides radioprotection to the intestinal epithelium
    • Egan LJ, Eckmann L, Greten FR, Chae S, Li ZW, Myhre GM et al. IκB-kinaseβdependent NF-κB activation provides radioprotection to the intestinal epithelium. Proc Natl Acad Sci USA 2004; 101: 2452-2457.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2452-2457
    • Egan, L.J.1    Eckmann, L.2    Greten, F.R.3    Chae, S.4    Li, Z.W.5    Myhre, G.M.6
  • 111
    • 0344496062 scopus 로고    scopus 로고
    • IKKβ is required for prevention of apoptosis mediated by cell-bound but not by circulating TNFα
    • Maeda S, Chang L, Li ZW, Luo JL, Leffert H, Karin M. IKKβ is required for prevention of apoptosis mediated by cell-bound but not by circulating TNFα. Immunity 2003; 19: 725-737.
    • (2003) Immunity , vol.19 , pp. 725-737
    • Maeda, S.1    Chang, L.2    Li, Z.W.3    Luo, J.L.4    Leffert, H.5    Karin, M.6
  • 112
    • 0034745021 scopus 로고    scopus 로고
    • IKKβ is essential for protecting T cells from TNFα-induced apoptosis
    • Senftleben U, Li ZW, Baud V, Karin M. IKKβ is essential for protecting T cells from TNFα-induced apoptosis. Immunity 2001; 14: 217-230.
    • (2001) Immunity , vol.14 , pp. 217-230
    • Senftleben, U.1    Li, Z.W.2    Baud, V.3    Karin, M.4
  • 113
    • 24944554790 scopus 로고    scopus 로고
    • Signaling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-κB as key regulators
    • Park JM, Greten FR, Wong A, Westrick RJ, Arthur JS, Otsu K et al. Signaling pathways and genes that inhibit pathogen-induced macrophage apoptosis - CREB and NF-κB as key regulators. Immunity 2005; 23: 319-329.
    • (2005) Immunity , vol.23 , pp. 319-329
    • Park, J.M.1    Greten, F.R.2    Wong, A.3    Westrick, R.J.4    Arthur, J.S.5    Otsu, K.6
  • 115
    • 0033634663 scopus 로고    scopus 로고
    • Female mice heterozygous for IKK γ/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti
    • Makris C, Godfrey VL, Krahn-Senftleben G, Takahashi T, Roberts JL, Schwarz T et al. Female mice heterozygous for IKK γ/NEMO deficiencies develop a dermatopathy similar to the human X-linked disorder incontinentia pigmenti. Mol Cell 2000; 5: 969-979.
    • (2000) Mol Cell , vol.5 , pp. 969-979
    • Makris, C.1    Godfrey, V.L.2    Krahn-Senftleben, G.3    Takahashi, T.4    Roberts, J.L.5    Schwarz, T.6
  • 116
    • 32144450234 scopus 로고    scopus 로고
    • Skin lesion development in a mouse model of incontinentia pigmenti is triggered by NEMO deficiency in epidermal keratinocytes and requires TNF signaling
    • Nenci A, Huth M, Funteh A, Schmidt-Supprian M, Bloch W, Metzger D et al. Skin lesion development in a mouse model of incontinentia pigmenti is triggered by NEMO deficiency in epidermal keratinocytes and requires TNF signaling. Hum Mol Genet 2006; 15: 531-542.
    • (2006) Hum Mol Genet , vol.15 , pp. 531-542
    • Nenci, A.1    Huth, M.2    Funteh, A.3    Schmidt-Supprian, M.4    Bloch, W.5    Metzger, D.6
  • 118
    • 33846839443 scopus 로고    scopus 로고
    • Deletion of NEMO/IKKγ in liver parenchymal cells causes steatohepatitis and hepatocellular carcinoma
    • Luedde T, Beraza N, Kotsikoris V, van Loo G, Nenci A, De Vos R et al. Deletion of NEMO/IKKγ in liver parenchymal cells causes steatohepatitis and hepatocellular carcinoma. Cancer Cell 2007; 11: 119-132.
    • (2007) Cancer Cell , vol.11 , pp. 119-132
    • Luedde, T.1    Beraza, N.2    Kotsikoris, V.3    Van Loo, G.4    Nenci, A.5    De Vos, R.6
  • 119
    • 33646713486 scopus 로고    scopus 로고
    • The TGFβ activated kinase TAK1 regulates vascular development in vivo
    • Jadrich JL, O'Connor MB, Coucouvanis E. The TGFβ activated kinase TAK1 regulates vascular development in vivo. Development 2006; 133: 1529-1541.
    • (2006) Development , vol.133 , pp. 1529-1541
    • Jadrich, J.L.1    O'Connor, M.B.2    Coucouvanis, E.3
  • 121
    • 0036895537 scopus 로고    scopus 로고
    • Targeted disruption of the Tab1 gene causes embryonic lethality and defects in cardiovascular and lung morphogenesis
    • Komatsu Y, Shibuya H, Takeda N, Ninomiya-Tsuji J, Yasui T, Miyado K et al. Targeted disruption of the Tab1 gene causes embryonic lethality and defects in cardiovascular and lung morphogenesis. Mech Dev 2002; 119: 239-249.
    • (2002) Mech Dev , vol.119 , pp. 239-249
    • Komatsu, Y.1    Shibuya, H.2    Takeda, N.3    Ninomiya-Tsuji, J.4    Yasui, T.5    Miyado, K.6
  • 122
    • 0037313041 scopus 로고    scopus 로고
    • TAB2 is essential for prevention of apoptosis in fetal liver but not for interleukin-1 signaling
    • Sanjo H, Takeda K, Tsujimura T, Ninomiya-Tsuji J, Matsumoto K, Akira S. TAB2 is essential for prevention of apoptosis in fetal liver but not for interleukin-1 signaling. Mol Cell Biol 2003; 23: 1231-1238.
    • (2003) Mol Cell Biol , vol.23 , pp. 1231-1238
    • Sanjo, H.1    Takeda, K.2    Tsujimura, T.3    Ninomiya-Tsuji, J.4    Matsumoto, K.5    Akira, S.6
  • 123
    • 84875996333 scopus 로고    scopus 로고
    • Essential roles of K63-linked polyubiquitin-binding proteins TAB2 and TAB3 in B cell activation via MAPKs
    • Ori D, Kato H, Sanjo H, Tartey S, Mino T, Akira S et al. Essential roles of K63-linked polyubiquitin-binding proteins TAB2 and TAB3 in B cell activation via MAPKs. J Immunol 2013; 190: 4037-4045.
    • (2013) J Immunol , vol.190 , pp. 4037-4045
    • Ori, D.1    Kato, H.2    Sanjo, H.3    Tartey, S.4    Mino, T.5    Akira, S.6
  • 124
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally
    • Varfolomeev EE, Schuchmann M, Luria V, Chiannilkulchai N, Beckmann JS, Mett IL et al. Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 1998; 9: 267-276.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3    Chiannilkulchai, N.4    Beckmann, J.S.5    Mett, I.L.6
  • 126
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activationinduced T-cell proliferation are defective in mice lacking FADD/Mort1
    • Zhang J, Cado D, Chen A, Kabra NH, Winoto A. Fas-mediated apoptosis and activationinduced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 1998; 392: 296-300.
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 127
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Yeh WC, de la Pompa JL, McCurrach ME, Shu HB, Elia AJ, Shahinian A et al. FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science 1998; 279: 1954-1958.
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    De La-Pompa, J.L.2    McCurrach, M.E.3    Shu, H.B.4    Elia, A.J.5    Shahinian, A.6
  • 128
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • Yeh WC, Itie A, Elia AJ, Ng M, Shu HB, Wakeham A et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity 2000; 12: 633-642.
    • (2000) Immunity , vol.12 , pp. 633-642
    • Yeh, W.C.1    Itie, A.2    Elia, A.J.3    Ng, M.4    Shu, H.B.5    Wakeham, A.6
  • 130
    • 84888237474 scopus 로고    scopus 로고
    • Cellular FLICE-like inhibitory protein secures intestinal epithelial cell survival and immune homeostasis by regulating caspase-8
    • Wittkopf N, Gunther C, Martini E, He G, Amann K, He YW et al. Cellular FLICE-like inhibitory protein secures intestinal epithelial cell survival and immune homeostasis by regulating caspase-8. Gastroenterology 2013; 145: 1369-1379.
    • (2013) Gastroenterology , vol.145 , pp. 1369-1379
    • Wittkopf, N.1    Gunther, C.2    Martini, E.3    He, G.4    Amann, K.5    He, Y.W.6
  • 131
    • 81355149658 scopus 로고    scopus 로고
    • Ablation of c-FLIP in hepatocytes enhances death-receptor mediated apoptosis and toxic liver injury in vivo
    • Schattenberg JM, Zimmermann T, Worns M, Sprinzl MF, Kreft A, Kohl T et al. Ablation of c-FLIP in hepatocytes enhances death-receptor mediated apoptosis and toxic liver injury in vivo. J Hepatol 2011; 55: 1272-1280.
    • (2011) J Hepatol , vol.55 , pp. 1272-1280
    • Schattenberg, J.M.1    Zimmermann, T.2    Worns, M.3    Sprinzl, M.F.4    Kreft, A.5    Kohl, T.6
  • 132
    • 78649731663 scopus 로고    scopus 로고
    • FLIP: A novel regulator of macrophage differentiation and granulocyte homeostasis
    • Huang QQ, Perlman H, Huang Z, Birkett R, Kan L, Agrawal H et al. FLIP: a novel regulator of macrophage differentiation and granulocyte homeostasis. Blood 2010; 116: 4968-4977.
    • (2010) Blood , vol.116 , pp. 4968-4977
    • Huang, Q.Q.1    Perlman, H.2    Huang, Z.3    Birkett, R.4    Kan, L.5    Agrawal, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.