메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Differential affinity of FLIP and procaspase 8 for FADD's DED binding surfaces regulates DISC assembly

Author keywords

[No Author keywords available]

Indexed keywords

DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEIN; DEATH RECEPTOR; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FLICE INHIBITORY PROTEIN; PROCASPASE 8; TRIPARTITE MOTIF PROTEIN 5; CASPASE 8; FADD PROTEIN, HUMAN; PROTEIN BINDING;

EID: 84896890429     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4350     Document Type: Article
Times cited : (67)

References (41)
  • 1
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • DOI 10.1016/S0092-8674(00)80564-4
    • Vaux, D. L. & Korsmeyer, S. J. Cell death in development. Cell 96, 245-254 (1999). (Pubitemid 29059354)
    • (1999) Cell , vol.96 , Issue.2 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 2
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson, M. P. Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1, 120-129 (2000).
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 3
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan, D. & Weinberg, R. A. Hallmarks of cancer: the next generation. Cell 144, 646-674 (2011).
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 4
    • 79952438496 scopus 로고    scopus 로고
    • Harnessing programmed cell death as a therapeutic strategy in rheumatic diseases
    • Ramaswamy, M., Deng, M. & Siegel, R. M. Harnessing programmed cell death as a therapeutic strategy in rheumatic diseases. Nat. Rev. Rheumatol. 7, 152-160 (2011).
    • (2011) Nat. Rev. Rheumatol. , vol.7 , pp. 152-160
    • Ramaswamy, M.1    Deng, M.2    Siegel, R.M.3
  • 5
    • 39749182234 scopus 로고    scopus 로고
    • Apoptosis: Controlled demolition at the cellular level
    • DOI 10.1038/nrm2312, PII NRM2312
    • Taylor, R. C., Cullen, S. P. & Martin, S. J. Apoptosis: controlled demolition at the cellular level. Nat. Rev. Mol. Cell Biol. 9, 231-241 (2008). (Pubitemid 351301823)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.3 , pp. 231-241
    • Taylor, R.C.1    Cullen, S.P.2    Martin, S.J.3
  • 6
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • DOI 10.1042/BJ20041142
    • Fuentes-Prior, P. & Salvesen, G. S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384, 201-232 (2004). (Pubitemid 39656233)
    • (2004) Biochemical Journal , vol.384 , Issue.2 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 10
    • 0037009370 scopus 로고    scopus 로고
    • Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8
    • DOI 10.1093/emboj/cdf441
    • Sprick, M. R. et al. Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8. EMBO J. 21, 4520-4530 (2002). (Pubitemid 34984339)
    • (2002) EMBO Journal , vol.21 , Issue.17 , pp. 4520-4530
    • Sprick, M.R.1    Rieser, E.2    Stahl, H.3    Grosse-Wilde, A.4    Weigand, M.A.5    Walczak, H.6
  • 11
    • 84876085177 scopus 로고    scopus 로고
    • Targeting c-FLIP in cancer
    • Shirley, S. & Micheau, O. Targeting c-FLIP in cancer. Cancer Lett. 332, 141-150 (2013).
    • (2013) Cancer Lett. , vol.332 , pp. 141-150
    • Shirley, S.1    Micheau, O.2
  • 12
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin, M. P. et al. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J. Biol. Chem. 270, 7795-7798 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 7795-7798
    • Boldin, M.P.1
  • 13
    • 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 114, 181-190 (2003). (Pubitemid 36936912)
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 14
    • 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
  • 15
    • 60549106191 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure unravels signalling by receptor clustering
    • Scott, F. L. et al. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 457, 1019-1022 (2009).
    • (2009) Nature , vol.457 , pp. 1019-1022
    • Scott, F.L.1
  • 17
    • 0035824635 scopus 로고    scopus 로고
    • Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8
    • Kischkel, F. C. et al. Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J. Biol. Chem. 276, 46639-46646 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 46639-46646
    • Kischkel, F.C.1
  • 21
    • 0033556310 scopus 로고    scopus 로고
    • The role of c-FLIP in modulation of CD95-induced apoptosis
    • Scaffidi, C., Schmitz, I., Krammer, P. H. & Peter, M. E. The role of c-FLIP in modulation of CD95-induced apoptosis. J. Biol. Chem. 274, 1541-1548 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1541-1548
    • Scaffidi, C.1    Schmitz, I.2    Krammer, P.H.3    Peter, M.E.4
  • 22
    • 68349154339 scopus 로고    scopus 로고
    • Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival
    • Hughes, M. A. et al. Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival. Mol. Cell 35, 265-279 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 265-279
    • Hughes, M.A.1
  • 23
    • 77952784381 scopus 로고    scopus 로고
    • Inducible dimerization and inducible cleavage reveal a requirement for both processes in caspase-8 activation
    • Oberst, A. et al. Inducible dimerization and inducible cleavage reveal a requirement for both processes in caspase-8 activation. J. Biol. Chem. 285, 16632-16642 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 16632-16642
    • Oberst, A.1
  • 24
    • 78549236456 scopus 로고    scopus 로고
    • The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
    • Wang, L. et al. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat. Struct. Mol. Biol. 17, 1324-1329 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1324-1329
    • Wang, L.1
  • 25
    • 84864318803 scopus 로고    scopus 로고
    • A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death
    • Dickens, L. S. et al. A death effector domain chain DISC model reveals a crucial role for caspase-8 chain assembly in mediating apoptotic cell death. Mol. Cell 47, 291-305 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 291-305
    • Dickens, L.S.1
  • 26
    • 84864294821 scopus 로고    scopus 로고
    • Stoichiometry of the CD95 death-inducing signaling complex: Experimental and modeling evidence for a death effector domain chain model
    • Schleich, K. et al. Stoichiometry of the CD95 death-inducing signaling complex: experimental and modeling evidence for a death effector domain chain model. Mol. Cell 47, 306-319 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 306-319
    • Schleich, K.1
  • 27
    • 77952912435 scopus 로고    scopus 로고
    • Conatumumab, a fully human agonist antibody to death receptor 5, induces apoptosis via caspase activation in multiple tumor types
    • Kaplan-Lefko, P. J. et al. Conatumumab, a fully human agonist antibody to death receptor 5, induces apoptosis via caspase activation in multiple tumor types. Cancer Biol. Ther. 9, 618-631 (2010).
    • (2010) Cancer Biol. Ther. , vol.9 , pp. 618-631
    • Kaplan-Lefko, P.J.1
  • 28
    • 84859479271 scopus 로고    scopus 로고
    • Vorinostat/SAHA-induced apoptosis in malignant mesothelioma is FLIP/caspase 8-dependent and HR23B-independent
    • Hurwitz, J. L. et al. Vorinostat/SAHA-induced apoptosis in malignant mesothelioma is FLIP/caspase 8-dependent and HR23B-independent. Eur. J. Cancer 48, 1096-1107 (2012).
    • (2012) Eur. J. Cancer , vol.48 , pp. 1096-1107
    • Hurwitz, J.L.1
  • 29
    • 29144463250 scopus 로고    scopus 로고
    • Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition
    • DOI 10.1016/j.molcel.2005.10.023, PII S1097276505017181
    • Yang, J. K. et al. Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition. Mol. Cell 20, 939-949 (2005). (Pubitemid 41814882)
    • (2005) Molecular Cell , vol.20 , Issue.6 , pp. 939-949
    • Yang, J.K.1    Wang, L.2    Zheng, L.3    Wan, F.4    Ahmed, M.5    Lenardo, M.J.6    Wu, H.7
  • 30
    • 33646377433 scopus 로고    scopus 로고
    • Crystal structure of a viral FLIP: Insights into FLIP-mediated inhibition of death receptor signaling
    • DOI 10.1074/jbc.M511074200
    • Li, F. Y., Jeffrey, P. D., Yu, J. W. & Shi, Y. Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling. J. Biol. Chem. 281, 2960-2968 (2006). (Pubitemid 43845763)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.5 , pp. 2960-2968
    • Li, F.-Y.1    Jeffrey, P.D.2    Yu, J.W.3    Shi, Y.4
  • 31
    • 40949149811 scopus 로고    scopus 로고
    • R, the only murine short FLIP isoform, reveal requirements for DISC recruitment
    • DOI 10.1038/sj.cdd.4402314, PII 4402314, The biology of Hypoxia-inducible factors
    • Ueffing, N. et al. Mutational analyses of c-FLIPR, the only murine short FLIP isoform, reveal requirements for DISC recruitment. Cell Death Differ. 15, 773-782 (2008). (Pubitemid 351405082)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.4 , pp. 773-782
    • Ueffing, N.1    Keil, E.2    Freund, C.3    Kuhne, R.4    Schulze-Osthoff, K.5    Schmitz, I.6
  • 32
    • 82755198022 scopus 로고    scopus 로고
    • Proliferative versus apoptotic functions of caspase-8 Hetero or homo: The caspase-8 dimer controls cell fate
    • van Raam, B. J. & Salvesen, G. S. Proliferative versus apoptotic functions of caspase-8 Hetero or homo: the caspase-8 dimer controls cell fate. Biochim. Biophys. Acta 1824, 113-122 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 113-122
    • Van Raam, B.J.1    Salvesen, G.S.2
  • 33
    • 0036139833 scopus 로고    scopus 로고
    • Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function
    • DOI 10.1128/JVI.76.2.697-706.2002
    • Garvey, T. L. et al. Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function. J. Virol. 76, 697-706 (2002). (Pubitemid 34033368)
    • (2002) Journal of Virology , vol.76 , Issue.2 , pp. 697-706
    • Garvey, T.L.1    Bertin, J.2    Siegel, R.M.3    Wang, G.-H.4    Lenardo, M.J.5    Cohen, J.I.6
  • 35
    • 78549275798 scopus 로고    scopus 로고
    • Unleashing cell death: The Fas-FADD complex
    • Hymowitz, S. G. & Dixit, V. M. Unleashing cell death: the Fas-FADD complex. Nat. Struct. Mol. Biol. 17, 1289-1290 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1289-1290
    • Hymowitz, S.G.1    Dixit, V.M.2
  • 36
    • 77955465116 scopus 로고    scopus 로고
    • Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL
    • Fricker, N. et al. Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL. J. Cell Biol. 190, 377-389 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 377-389
    • Fricker, N.1
  • 37
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A. & Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993). (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 38
    • 63049089877 scopus 로고    scopus 로고
    • Death effector domain-containing proteins
    • Valmiki, M. G. & Ramos, J. W. Death effector domain-containing proteins. Cell Mol. Life. Sci. 66, 814-830 (2009).
    • (2009) Cell Mol. Life. Sci. , vol.66 , pp. 814-830
    • Valmiki, M.G.1    Ramos, J.W.2
  • 40
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • DOI 10.1002/prot.340170404
    • Sippl, M. J. Recognition of errors in three-dimensional structures of proteins. Proteins 17, 355-362 (1993). (Pubitemid 23358545)
    • (1993) Proteins: Structure, Function and Genetics , vol.17 , Issue.4 , pp. 355-362
    • Sippl, M.J.1
  • 41
    • 77957242885 scopus 로고    scopus 로고
    • Ultra-fast FFT protein docking on graphics processors
    • Ritchie, D. W. & Venkatraman, V. Ultra-fast FFT protein docking on graphics processors. Bioinformatics 26, 2398-2405 (2010).
    • (2010) Bioinformatics , vol.26 , pp. 2398-2405
    • Ritchie, D.W.1    Venkatraman, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.