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Volumn 457, Issue 7232, 2009, Pages 1019-1022

The Fas-FADD death domain complex structure unravels signalling by receptor clustering

Author keywords

[No Author keywords available]

Indexed keywords

FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; OLIGOMER; TETRAMER;

EID: 60549106191     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07606     Document Type: Article
Times cited : (316)

References (30)
  • 1
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi, A. & Dixit, V. M. Apoptosis control by death and decoy receptors. Curr. Opin. Cell Biol. 11, 255-260 (1999).
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 2
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • Peter, M. E. & Krammer, P. H. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ. 10, 26-35 (2003).
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 4
    • 0034644508 scopus 로고    scopus 로고
    • Insights into programmed cell death through structural biology
    • Fesik, S. W. Insights into programmed cell death through structural biology. Cell 103, 273-282 (2000).
    • (2000) Cell , vol.103 , pp. 273-282
    • Fesik, S.W.1
  • 5
    • 34247842740 scopus 로고    scopus 로고
    • The death domain superfamily in intracellular signaling of apoptosis and inflammation
    • Park, H. H. et al. The death domain superfamily in intracellular signaling of apoptosis and inflammation. Annu. Rev. Immunol. 25, 561-586 (2007).
    • (2007) Annu. Rev. Immunol , vol.25 , pp. 561-586
    • Park, H.H.1
  • 6
    • 33746921690 scopus 로고    scopus 로고
    • Caspase-containing complexes in the regulation of cell death and inflammation
    • Festjens, N., Cornelis, S., Lamkanfi, M. & Vandenabeele, P. Caspase-containing complexes in the regulation of cell death and inflammation. Biol. Chem. 387, 1005-1016 (2006).
    • (2006) Biol. Chem , vol.387 , pp. 1005-1016
    • Festjens, N.1    Cornelis, S.2    Lamkanfi, M.3    Vandenabeele, P.4
  • 7
    • 0038393124 scopus 로고    scopus 로고
    • The death effector domain protein family: Regulators of cellular homeostasis
    • Tibbetts, M. D., Zheng, L. & Lenardo, M. J. The death effector domain protein family: regulators of cellular homeostasis. Nature Immunol. 4, 404-409 (2003).
    • (2003) Nature Immunol , vol.4 , pp. 404-409
    • Tibbetts, M.D.1    Zheng, L.2    Lenardo, M.J.3
  • 8
    • 0036133127 scopus 로고    scopus 로고
    • Molecular ordering of the initial signaling events of CD95
    • Algeciras-Schimnich, A. et al. Molecular ordering of the initial signaling events of CD95. Mol. Cell. Biol. 22, 207-220 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 207-220
    • Algeciras-Schimnich, A.1
  • 9
    • 33846247103 scopus 로고    scopus 로고
    • Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling
    • Feig, C., Tchikov, V., Schutze, S. & Peter, M. E. Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling. EMBO J. 26, 221-231 (2007).
    • (2007) EMBO J , vol.26 , pp. 221-231
    • Feig, C.1    Tchikov, V.2    Schutze, S.3    Peter, M.E.4
  • 10
    • 34250346095 scopus 로고    scopus 로고
    • Analysis of CD95 threshold signaling: Triggering of CD95 (FAS/ APO-1) at low concentrations primarily results in survival signaling
    • Lavrik, I. N. et al. Analysis of CD95 threshold signaling: triggering of CD95 (FAS/ APO-1) at low concentrations primarily results in survival signaling. J. Biol. Chem. 282, 13664-13671 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 13664-13671
    • Lavrik, I.N.1
  • 11
    • 1142287412 scopus 로고    scopus 로고
    • Ligand-independent redistribution of Fas (CD95) into lipid rafts mediates clonotypic T cell death
    • Muppidi, J. R. & Siegel, R. M. Ligand-independent redistribution of Fas (CD95) into lipid rafts mediates clonotypic T cell death. Nature Immunol. 5, 182-189 (2004).
    • (2004) Nature Immunol , vol.5 , pp. 182-189
    • Muppidi, J.R.1    Siegel, R.M.2
  • 12
    • 3543125877 scopus 로고    scopus 로고
    • Modifications and intracellular trafficking of FADD/MORT1 and caspase-8 after stimulation of T lymphocytes
    • O'Reilly, L. A. et al. Modifications and intracellular trafficking of FADD/MORT1 and caspase-8 after stimulation of T lymphocytes. Cell Death Differ. 11, 724-736 (2004).
    • (2004) Cell Death Differ , vol.11 , pp. 724-736
    • O'Reilly, L.A.1
  • 13
    • 9444268061 scopus 로고    scopus 로고
    • SPOTS: Signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane
    • Siegel, R. M. et al. SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane. J. Cell Biol. 167, 735-744 (2004).
    • (2004) J. Cell Biol , vol.167 , pp. 735-744
    • Siegel, R.M.1
  • 14
    • 33751213356 scopus 로고    scopus 로고
    • Emerging roles for the death adaptor FADD in death receptor avidity and cell cycle regulation
    • Werner, M. H., Wu, C. & Walsh, C. M. Emerging roles for the death adaptor FADD in death receptor avidity and cell cycle regulation. Cell Cycle 5, 2332-2338 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 2332-2338
    • Werner, M.H.1    Wu, C.2    Walsh, C.M.3
  • 15
    • 36849045915 scopus 로고    scopus 로고
    • The inflammasome: A danger sensing complex triggering innate immunity
    • Petrilli, V., Dostert, C., Muruve, D. A. & Tschopp, J. The inflammasome: a danger sensing complex triggering innate immunity. Curr. Opin. Immunol. 19, 615-622 (2007).
    • (2007) Curr. Opin. Immunol , vol.19 , pp. 615-622
    • Petrilli, V.1    Dostert, C.2    Muruve, D.A.3    Tschopp, J.4
  • 16
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • Riedl, S. J. & Salvesen, G. S. The apoptosome: signalling platform of cell death. Nature Rev. Mol. Cell Biol. 8, 405-413 (2007).
    • (2007) Nature Rev. Mol. Cell Biol , vol.8 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 17
    • 0034622940 scopus 로고    scopus 로고
    • The three-dimensional solution structure and dynamic properties of the human FADD death domain
    • Berglund, H. et al. The three-dimensional solution structure and dynamic properties of the human FADD death domain. J. Mol. Biol. 302, 171-188 (2000).
    • (2000) J. Mol. Biol , vol.302 , pp. 171-188
    • Berglund, H.1
  • 18
    • 33744539048 scopus 로고    scopus 로고
    • The structure of FADD and its mode of interaction with procaspase-8
    • Carrington, P. E. et al. The structure of FADD and its mode of interaction with procaspase-8. Mol. Cell 22, 599-610 (2006).
    • (2006) Mol. Cell , vol.22 , pp. 599-610
    • Carrington, P.E.1
  • 19
    • 0033522889 scopus 로고    scopus 로고
    • The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD
    • Jeong, E. J. et al. The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. J. Biol. Chem. 274, 16337-16342 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 16337-16342
    • Jeong, E.J.1
  • 20
    • 0030465072 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
    • Huang, B., Eberstadt, M., Olejniczak, E. T., Meadows, R. P. & Fesik, S. W. NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain. Nature 384, 638-641 (1996).
    • (1996) Nature , vol.384 , pp. 638-641
    • Huang, B.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Fesik, S.W.5
  • 21
    • 0028916599 scopus 로고    scopus 로고
    • Clackson, T. & Wells, J. A. A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386 (1995).
    • Clackson, T. & Wells, J. A. A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386 (1995).
  • 23
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A. A. & Thorn, K. S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9 (1998).
    • (1998) J. Mol. Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 24
    • 0036931719 scopus 로고    scopus 로고
    • Solvent exposed non-contacting amino acids play a critical role in NF-κB/IκBα complex formation
    • Huxford, T. et al. Solvent exposed non-contacting amino acids play a critical role in NF-κB/IκBα complex formation. J. Mol. Biol. 324, 587-597 (2002).
    • (2002) J. Mol. Biol , vol.324 , pp. 587-597
    • Huxford, T.1
  • 25
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S. & Chothia, C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204, 155-164 (1988).
    • (1988) J. Mol. Biol , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 26
    • 25144452720 scopus 로고    scopus 로고
    • Mutational analysis of the IFNAR1 binding site on IFNα2 reveals the architecture of a weak ligand-receptor binding-site
    • Roisman, L. C., Jaitin, D. A., Baker, D. P. & Schreiber, G. Mutational analysis of the IFNAR1 binding site on IFNα2 reveals the architecture of a weak ligand-receptor binding-site. J. Mol. Biol. 353, 271-281 (2005).
    • (2005) J. Mol. Biol , vol.353 , pp. 271-281
    • Roisman, L.C.1    Jaitin, D.A.2    Baker, D.P.3    Schreiber, G.4
  • 27
    • 34548050438 scopus 로고    scopus 로고
    • Biophysical and cell-based evidence for differential interactions between the death domains of CD95/Fas and FADD
    • Ferguson, B. J. et al. Biophysical and cell-based evidence for differential interactions between the death domains of CD95/Fas and FADD. Cell Death Differ. 14, 1717-1719 (2007).
    • (2007) Cell Death Differ , vol.14 , pp. 1717-1719
    • Ferguson, B.J.1
  • 28
    • 0027281373 scopus 로고
    • A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen
    • Itoh, N. & Nagata, S. A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen. J. Biol. Chem. 268, 10932-10937 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 10932-10937
    • Itoh, N.1    Nagata, S.2
  • 29
    • 27644505459 scopus 로고    scopus 로고
    • Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1
    • Kim, H. E., Du, F., Fang, M. & Wang, X. Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proc. Natl Acad. Sci. USA 102, 17545-17550 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17545-17550
    • Kim, H.E.1    Du, F.2    Fang, M.3    Wang, X.4
  • 30
    • 0037291871 scopus 로고    scopus 로고
    • A unified model for apical caspase activation
    • Boatright, K. M. et al. A unified model for apical caspase activation. Mol. Cell 11, 529-541 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 529-541
    • Boatright, K.M.1


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