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Volumn 312, Issue 11, 2006, Pages 2142-2153

TNF-receptor I defective in internalization allows for cell death through activation of neutral sphingomyelinase

Author keywords

Apoptosis; Caspase; Cathepsin D; DISC; Sphingomyelinase; TNF RI

Indexed keywords

CASPASE 3; CASPASE 9; SPHINGOMYELIN PHOSPHODIESTERASE; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR 1; CASP3 PROTEIN, MOUSE; CASP9 PROTEIN, MOUSE; CASPASE; CERAMIDE; DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEIN; DEDD PROTEIN, MOUSE; DNA BINDING PROTEIN; NSMAF PROTEIN, MOUSE; SIGNAL PEPTIDE; SMALL INTERFERING RNA; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR 2;

EID: 33746690768     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.03.014     Document Type: Article
Times cited : (38)

References (35)
  • 1
    • 0035936797 scopus 로고    scopus 로고
    • The TNF and TNF receptor superfamilies: integrating mammalian biology
    • Locksley R.M., Killeen N., and Lenardo M.J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104 (2001) 487-501
    • (2001) Cell , vol.104 , pp. 487-501
    • Locksley, R.M.1    Killeen, N.2    Lenardo, M.J.3
  • 3
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: a double-edged sword
    • Aggarwal B.B. Signalling pathways of the TNF superfamily: a double-edged sword. Nat. Rev., Immunol. 3 (2003) 745-756
    • (2003) Nat. Rev., Immunol. , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 4
    • 0027275490 scopus 로고
    • A novel domain within the 55 kD TNF receptor signals cell death
    • Tartaglia L.A., Ayres T.M., Wong G.H., and Goeddel D.V. A novel domain within the 55 kD TNF receptor signals cell death. Cell 74 (1993) 845-853
    • (1993) Cell , vol.74 , pp. 845-853
    • Tartaglia, L.A.1    Ayres, T.M.2    Wong, G.H.3    Goeddel, D.V.4
  • 5
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • Hsu H., Xiong J., and Goeddel D.V. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell 81 (1995) 495-504
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 6
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H., Huang J., Shu H.B., Baichwal V., and Goeddel D.V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4 (1996) 387-396
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 7
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu H., Shu H.B., Pan M.G., and Goeddel D.V. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84 (1996) 299-308
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shu, H.B.2    Pan, M.G.3    Goeddel, D.V.4
  • 8
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin M.P., Goncharov T.M., Goltsev Y.V., and Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85 (1996) 803-815
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 11
    • 0033538073 scopus 로고    scopus 로고
    • Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling
    • Schütze S., Machleidt T., Adam D., Schwandner R., Wiegmann K., Kruse M.L., Heinrich M., Wickel M., and Krönke M. Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling. J. Biol. Chem. 274 (1999) 10203-10212
    • (1999) J. Biol. Chem. , vol.274 , pp. 10203-10212
    • Schütze, S.1    Machleidt, T.2    Adam, D.3    Schwandner, R.4    Wiegmann, K.5    Kruse, M.L.6    Heinrich, M.7    Wickel, M.8    Krönke, M.9
  • 12
    • 15844383383 scopus 로고    scopus 로고
    • A novel cytoplasmic domain of the p55 tumor necrosis factor receptor initiates the neutral sphingomyelinase pathway
    • Adam D., Wiegmann K., Adam-Klages S., Ruff A., and Krönke M. A novel cytoplasmic domain of the p55 tumor necrosis factor receptor initiates the neutral sphingomyelinase pathway. J. Biol. Chem. 271 (1996) 14617-14622
    • (1996) J. Biol. Chem. , vol.271 , pp. 14617-14622
    • Adam, D.1    Wiegmann, K.2    Adam-Klages, S.3    Ruff, A.4    Krönke, M.5
  • 14
    • 0033529534 scopus 로고    scopus 로고
    • Differential modulation of apoptosis sensitivity in CD95 type I and type II cells
    • Scaffidi C., Schmitz I., Zha J., Korsmeyer S.J., Krammer P.H., and Peter M.E. Differential modulation of apoptosis sensitivity in CD95 type I and type II cells. J. Biol. Chem. 274 (1999) 22532-22538
    • (1999) J. Biol. Chem. , vol.274 , pp. 22532-22538
    • Scaffidi, C.1    Schmitz, I.2    Zha, J.3    Korsmeyer, S.J.4    Krammer, P.H.5    Peter, M.E.6
  • 15
    • 0034615555 scopus 로고    scopus 로고
    • Caspases-controlling intracellular signals by protease zymogen activation
    • Stennicke H.R., and Salvesen G.S. Caspases-controlling intracellular signals by protease zymogen activation. Biochim. Biophys. Acta 1477 (2000) 299-306
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 299-306
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 16
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., and Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 17
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., and Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94 (1998) 481-490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 18
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S., and Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10 (2000) 369-377
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 19
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., and Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 20
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha
    • Deiss L.P., Galinka H., Berissi H., Cohen O., and Kimchi A. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBO J. 15 (1996) 3861-3870
    • (1996) EMBO J. , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 22
    • 0036310279 scopus 로고    scopus 로고
    • Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts
    • Roberg K., Kagedal K., and Ollinger K. Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts. Am. J. Pathol. 161 (2002) 89-96
    • (2002) Am. J. Pathol. , vol.161 , pp. 89-96
    • Roberg, K.1    Kagedal, K.2    Ollinger, K.3
  • 24
    • 0032497837 scopus 로고    scopus 로고
    • The role of ceramide in cell signaling
    • Perry D.K., and Hannun Y.A. The role of ceramide in cell signaling. Biochim. Biophys. Acta 1436 (1998) 233-243
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 233-243
    • Perry, D.K.1    Hannun, Y.A.2
  • 25
    • 0038529730 scopus 로고    scopus 로고
    • Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism
    • Marchesini N., Luberto C., and Hannun Y.A. Biochemical properties of mammalian neutral sphingomyelinase 2 and its role in sphingolipid metabolism. J. Biol. Chem. 278 (2003) 13775-13783
    • (2003) J. Biol. Chem. , vol.278 , pp. 13775-13783
    • Marchesini, N.1    Luberto, C.2    Hannun, Y.A.3
  • 26
    • 0042197417 scopus 로고    scopus 로고
    • The TNF receptor 1: a split personality complex
    • Barnhart B.C., and Peter M.E. The TNF receptor 1: a split personality complex. Cell 114 (2003) 148-150
    • (2003) Cell , vol.114 , pp. 148-150
    • Barnhart, B.C.1    Peter, M.E.2
  • 27
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O., and Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114 (2003) 181-190
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 28
    • 0042466637 scopus 로고    scopus 로고
    • Interdimer processing mechanism of procaspase-8 activation
    • Chang D.W., Xing Z., Capacio V.L., Peter M.E., and Yang X. Interdimer processing mechanism of procaspase-8 activation. EMBO J. 22 (2003) 4132-4142
    • (2003) EMBO J. , vol.22 , pp. 4132-4142
    • Chang, D.W.1    Xing, Z.2    Capacio, V.L.3    Peter, M.E.4    Yang, X.5
  • 29
    • 13744253447 scopus 로고    scopus 로고
    • Caspases-at the cutting edge of cell death
    • Stennicke H.R. Caspases-at the cutting edge of cell death. Symp. Soc. Exp. Biol. 52 (2000) 13-29
    • (2000) Symp. Soc. Exp. Biol. , vol.52 , pp. 13-29
    • Stennicke, H.R.1
  • 30
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 (2004) 205-219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 31
    • 0033020265 scopus 로고    scopus 로고
    • Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis
    • Buendia B., Santa-Maria A., and Courvalin J.C. Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis. J. Cell Sci. 112 Pt. 11 (1999) 1743-1753
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 11 , pp. 1743-1753
    • Buendia, B.1    Santa-Maria, A.2    Courvalin, J.C.3
  • 32
    • 0031902779 scopus 로고    scopus 로고
    • Fas-induced DNA fragmentation and proteolysis of nuclear proteins
    • Kawahara A., Enari M., Talanian R.V., Wong W.W., and Nagata S. Fas-induced DNA fragmentation and proteolysis of nuclear proteins. Genes Cells 3 (1998) 297-306
    • (1998) Genes Cells , vol.3 , pp. 297-306
    • Kawahara, A.1    Enari, M.2    Talanian, R.V.3    Wong, W.W.4    Nagata, S.5
  • 33
    • 0037201939 scopus 로고    scopus 로고
    • Sphingomyelinases: enzymology and membrane activity
    • Goni F.M., and Alonso A. Sphingomyelinases: enzymology and membrane activity. FEBS Lett. 531 (2002) 38-46
    • (2002) FEBS Lett. , vol.531 , pp. 38-46
    • Goni, F.M.1    Alonso, A.2
  • 34
    • 0032518448 scopus 로고    scopus 로고
    • Role of an acidic compartment in tumor-necrosis-factor-alpha-induced production of ceramide, activation of caspase-3 and apoptosis
    • Monney L., Olivier R., Otter I., Jansen B., Poirier G.G., and Borner C. Role of an acidic compartment in tumor-necrosis-factor-alpha-induced production of ceramide, activation of caspase-3 and apoptosis. Eur. J. Biochem. 251 (1998) 295-303
    • (1998) Eur. J. Biochem. , vol.251 , pp. 295-303
    • Monney, L.1    Olivier, R.2    Otter, I.3    Jansen, B.4    Poirier, G.G.5    Borner, C.6
  • 35
    • 33744953581 scopus 로고    scopus 로고
    • Novel TNF-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein
    • (Epub ahead of print)
    • Krut O., Wiegmann K., Kashkar H., Yazdanpanah B., and Krönke M. Novel TNF-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein. J. Biol. Chem. (2006 (Mar 3)) (Epub ahead of print)
    • (2006) J. Biol. Chem.
    • Krut, O.1    Wiegmann, K.2    Kashkar, H.3    Yazdanpanah, B.4    Krönke, M.5


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