메뉴 건너뛰기




Volumn 2, Issue 11, 2011, Pages

TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex i and II members

Author keywords

A20; LUBAC; RIP1; TNF induced necroptosis

Indexed keywords

CASPASE 8; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NUCLEAR RECEPTOR COACTIVATOR 2; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR 1;

EID: 83155192804     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2011.111     Document Type: Article
Times cited : (192)

References (42)
  • 2
    • 0037815277 scopus 로고    scopus 로고
    • Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor I signaling complex during tumor necrosis factor-induced apoptosis
    • DOI 10.1074/jbc.M303399200
    • Harper N, Hughes M, MacFarlane M, Cohen GM. Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis. J Biol Chem 2003; 278: 25534-25541. (Pubitemid 36835305)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25534-25541
    • Harper, N.1    Hughes, M.2    MacFarlane, M.3    Cohen, G.M.4
  • 3
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • DOI 10.1016/S0092-8674(03)00521-X
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003; 114: 181-190. (Pubitemid 36936912)
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 4
    • 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
  • 6
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha 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 TNFalpha 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
  • 7
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]
    • Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation [corrected]. Nat Cell Biol 2006; 8: 398-406.
    • (2006) Nat 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
  • 10
    • 43049152912 scopus 로고    scopus 로고
    • TNF-α Induces Two Distinct Caspase-8 Activation Pathways
    • DOI 10.1016/j.cell.2008.03.036, PII S0092867408005011
    • Wang L, Du F, Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 2008; 133: 693-703. (Pubitemid 351636305)
    • (2008) Cell , vol.133 , Issue.4 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 11
    • 35548974703 scopus 로고    scopus 로고
    • Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD
    • DOI 10.1016/j.devcel.2007.09.007, PII S1534580707003486
    • Wright A, Reiley WW, Chang M, Jin W, Lee AJ, Zhang M et al. Regulation of early wave of germ cell apoptosis and spermatogenesis by deubiquitinating enzyme CYLD. Dev Cell 2007; 13: 705-716. (Pubitemid 350011985)
    • (2007) Developmental Cell , vol.13 , Issue.5 , pp. 705-716
    • Wright, A.1    Reiley, W.W.2    Chang, M.3    Jin, W.4    Lee, A.J.5    Zhang, M.6    Sun, S.-C.7
  • 12
    • 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
  • 13
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • DOI 10.1016/j.cellsig.2007.05.016, PII S089865680700157X
    • 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. (Pubitemid 47353808)
    • (2007) Cellular Signalling , vol.19 , Issue.10 , pp. 2056-2067
    • Feng, S.1    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.-e.5    Hoti, N.6    Castanares, M.7    Wu, M.8
  • 15
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler N, Zaru R, Micheau O, Thome M, Attinger A, Valitutti S et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol 2000; 1: 489-495.
    • (2000) Nat Immunol , vol.1 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3    Thome, M.4    Attinger, A.5    Valitutti, S.6
  • 17
    • 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
  • 19
    • 79952780505 scopus 로고    scopus 로고
    • Functional complementation between FADD and RIP1 in embryos and lymphocytes
    • Zhang H, Zhou X, McQuade T, Li J, Chan FK, Zhang J. Functional complementation between FADD and RIP1 in embryos and lymphocytes. Nature 2011; 471: 373-376.
    • (2011) Nature , vol.471 , pp. 373-376
    • Zhang, H.1    Zhou, X.2    McQuade, T.3    Li, J.4    Chan, F.K.5    Zhang, J.6
  • 21
    • 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
  • 23
    • 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
  • 25
    • 84856700215 scopus 로고    scopus 로고
    • Molecular definitions of cell death subroutines: Recommendations of the Nomenclature Committee on Cell Death 2012
    • e-pub ahead of print 15 July 2011
    • Galluzzi L, Vitale I, Abrams JM, Alnemri ES, Baehrecke EH, Blagosklonny MV et al. Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ 2011; e-pub ahead of print 15 July 2011.
    • (2011) Cell Death Differ
    • Galluzzi, L.1    Vitale, I.2    Abrams, J.M.3    Alnemri, E.S.4    Baehrecke, E.H.5    Blagosklonny, M.V.6
  • 26
    • 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
  • 27
    • 57649181391 scopus 로고    scopus 로고
    • Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway
    • Hitomi J, Christofferson DE, Ng A, Yao J, Degterev A, Xavier RJ et al. Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell 2008; 135: 1311-1323.
    • (2008) Cell , vol.135 , pp. 1311-1323
    • Hitomi, J.1    Christofferson, D.E.2    Ng, A.3    Yao, J.4    Degterev, A.5    Xavier, R.J.6
  • 28
    • 50149089360 scopus 로고    scopus 로고
    • The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors
    • Pobezinskaya YL, Kim YS, Choksi S, Morgan MJ, Li T, Liu C et al. The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors. Nat Immunol 2008; 9: 1047-1054.
    • (2008) Nat Immunol , vol.9 , pp. 1047-1054
    • Pobezinskaya, Y.L.1    Kim, Y.S.2    Choksi, S.3    Morgan, M.J.4    Li, T.5    Liu, C.6
  • 29
    • 50049125047 scopus 로고    scopus 로고
    • Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses
    • Ermolaeva MA, Michallet MC, Papadopoulou N, Utermohlen O, Kranidioti K, Kollias G et al. Function of TRADD in tumor necrosis factor receptor 1 signaling and in TRIF-dependent inflammatory responses. Nat Immunol 2008; 9: 1037-1046.
    • (2008) Nat Immunol , vol.9 , pp. 1037-1046
    • Ermolaeva, M.A.1    Michallet, M.C.2    Papadopoulou, N.3    Utermohlen, O.4    Kranidioti, K.5    Kollias, G.6
  • 30
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation
    • DOI 10.1016/S0092-8674(00)81466-X
    • Yamaoka S, Courtois G, Bessia C, Whiteside ST, Weil R, Agou F et al. Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 1998; 93: 1231-1240. (Pubitemid 28307427)
    • (1998) Cell , vol.93 , Issue.7 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6    Kirk, H.E.7    Kay, R.J.8    Israel, A.9
  • 34
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • 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-alpha. 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
  • 36
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of Hsp96 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-κB activation
    • DOI 10.1074/jbc.275.14.10519
    • Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 2000; 275: 10519-10526. (Pubitemid 30202115)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6    Liu, Z.-G.7
  • 37
  • 38
    • 33646234026 scopus 로고    scopus 로고
    • Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1
    • Zheng L, Bidere N, Staudt D, Cubre A, Orenstein J, Chan FK et al. Competitive control of independent programs of tumor necrosis factor receptor-induced cell death by TRADD and RIP1. Mol Cell Biol 2006; 26: 3505-3513.
    • (2006) Mol Cell Biol , vol.26 , pp. 3505-3513
    • Zheng, L.1    Bidere, N.2    Staudt, D.3    Cubre, A.4    Orenstein, J.5    Chan, F.K.6
  • 39
    • 0033452592 scopus 로고    scopus 로고
    • Inhibition of tumor necrosis factor-induced necrotic cell death by the zinc finger protein A20
    • Heyninck K, Denecker G, De Valck D, Fiers W, Beyaert R. Inhibition of tumor necrosis factor-induced necrotic cell death by the zinc finger protein A20. Anticancer Res 1999; 19 (4B): 2863-2868. (Pubitemid 30042563)
    • (1999) Anticancer Research , vol.19 , Issue.4 B , pp. 2863-2868
    • Heyninck, K.1    Denecker, G.2    De Valck, D.3    Fiers, W.4    Beyaert, R.5
  • 40
    • 60649110012 scopus 로고    scopus 로고
    • TNFalpha-induced macrophage death via caspase-dependent and independent pathways
    • Tran TM, Temkin V, Shi B, Pagliari L, Daniel S, Ferran C et al. TNFalpha-induced macrophage death via caspase-dependent and independent pathways. Apoptosis 2009; 14: 320-332.
    • (2009) Apoptosis , vol.14 , pp. 320-332
    • Tran, T.M.1    Temkin, V.2    Shi, B.3    Pagliari, L.4    Daniel, S.5    Ferran, C.6
  • 41
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-κB signal
    • DOI 10.1016/S1074-7613(00)80535-X
    • Kelliher MA, Grimm S, Ishida Y, Kuo F, Stanger BZ, Leder P. The death domain kinase RIP mediates the TNF-induced NF-kappaB signal. Immunity 1998; 8: 297-303. (Pubitemid 28188890)
    • (1998) Immunity , vol.8 , Issue.3 , pp. 297-303
    • Kelliher, M.A.1    Grimm, S.2    Ishida, Y.3    Kuo, F.4    Stanger, B.Z.5    Leder, P.6
  • 42
    • 79953906762 scopus 로고    scopus 로고
    • In TNF-stimulated cells, RIPK1 promotes cell survival by stabilizing TRAF2 and cIAP1, which limits induction of non-canonical NF-{kappa}B and activation of caspase-8
    • Gentle IE, Wong WW, Evans JM, Bankovacki A, Cook WD, Khan NR et al. In TNF-stimulated cells, RIPK1 promotes cell survival by stabilizing TRAF2 and cIAP1, which limits induction of non-canonical NF-{kappa}B and activation of caspase-8. J Biol Chem 2011; 286: 13282-13291.
    • (2011) J Biol Chem , vol.286 , pp. 13282-13291
    • Gentle, I.E.1    Wong, W.W.2    Evans, J.M.3    Bankovacki, A.4    Cook, W.D.5    Khan, N.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.