The death effector domain protein family: regulators of cellular homeostasis (original) (raw)

• Itoh, N. & Nagata, S. A novel protein domain required for apoptosis. Mutational analysis of human Fas antigen. J. Biol. Chem. 268, 10932–10937 (1993).
  CAS PubMed Google Scholar
• Tartaglia, L.A., Ayres, T.M., Wong, G.H. & Goeddel, D.V. A novel domain within the 55 kD TNF receptor signals cell death. Cell 74, 845–853 (1993).
  Article CAS PubMed Google Scholar
• 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).
  Article CAS PubMed Google Scholar
• Chinnaiyan, A.M., O'Rourke, K., Tewari, M. & Dixit, V.M. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81, 505–512 (1995).
  Article CAS PubMed Google Scholar
• Fernandes-Alnemri, T. et al. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc. Natl. Acad. Sci. USA 93, 7464–7469 (1996).
  Article CAS PubMed PubMed Central Google Scholar
• Muzio, M., Stockwell, B.R., Stennicke, H.R., Salvasen, G.S. & Dixit, V.M. An induced proximity model for caspase-8 activation. J. Biol. Chem. 273, 2926–2930 (1998).
  Article CAS PubMed Google Scholar
• 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).
  Article CAS PubMed Google Scholar
• Martin, D.A., Siegel, R.M., Zheng, L. & Lenardo, M.J. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHα1) death signal. J. Biol. Chem. 273, 4345–4349 (1998).
  Article CAS PubMed Google Scholar
• Wang, J., Chun, H.J., Wong, W., Spencer, D.M. & Lenardo, M.J. Caspase-10 is an initiator caspase in death receptor signaling. Proc. Natl. Acad. Sci. USA 98, 13884–13888 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Boldin, M.P., Goncharov, T.M., Goltsev, Y.V. & Wallach, D.I. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/Apo-1 and TNF receptor-induced cell death. Cell 85, 803–815 (1996).
  Article CAS PubMed Google Scholar
• Muzio, M. et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85, 817–827 (1996).
  Article CAS PubMed Google Scholar
• Weber, C.H. & Vincenz, C. The death domain superfamily: a tale of two interfaces? Trends Biochem. Sci. 26, 475–481 (2001).
  Article CAS PubMed Google Scholar
• Eberstadt, M. et al. NMR structure and mutagenesis of the FADD (MORT1) death-effector domain. Nature 392, 941–945 (1998).
  Article CAS PubMed Google Scholar
• Hofmann, K. The modular nature of apoptotic signaling proteins. Cell. Mol. Life Sci. 55, 1113–1128 (1999).
  Article CAS PubMed Google Scholar
• Martinon, F., Hofman, K. & Tschopp, J. The pyrin domain: a possible member of the death domain family implicated in apoptosis and inflammation. Curr. Biol. 11, R118–R120 (2001).
  Article CAS PubMed Google Scholar
• Hofmann, K., Bucher, P. & Tschopp, J. The CARD domain: a new apoptotic signalling motif. Trends Biochem. Sci. 22, 155–156 (1997).
  Article CAS PubMed Google Scholar
• 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).
  Article CAS PubMed PubMed Central Google Scholar
• Hu, S. & Yang, X. dFADD, a novel death domain-containing adapter protein for the Drosophila caspase DREDD. J. Biol. Chem. 275, 30761–30764 (2000).
  Article CAS PubMed Google Scholar
• Lee, S.W., Ko, Y.G., Bang, S., Kim, K.S. & Kim, S. Death effector domain of a mammalian apoptosis mediator, FADD, induces bacterial cell death. Mol. Microbiol. 35, 1540–1549 (2000).
  Article CAS PubMed Google Scholar
• Siegel, R.M. et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 288, 2354–2357 (2000).
  Article CAS PubMed Google Scholar
• Kaufmann, M. et al. Identification of a basic surface area of the FADD death effector domain critical for apoptotic signaling. FEBS Lett. 527, 250–254 (2002).
  Article CAS PubMed Google Scholar
• Weber, C.H. & Vincenz, C. A docking model of key components of the DISC complex: death domain superfamily interactions redefined. FEBS Lett. 492, 171–176 (2001).
  Article CAS PubMed Google Scholar
• Rieux-Laucat, F. et al. Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity. Science 268, 1347–1349 (1995).
  Article CAS PubMed Google Scholar
• Fisher, G.H. et al. Dominant interfering Fas gene mutations impair apoptosis in a human autoimmune lymphoproliferative syndrome. Cell 81, 935–946 (1995).
  Article CAS PubMed Google Scholar
• Sneller, M.C. et al. Clinical, immunologic, and genetic features of an autoimmune lymphoproliferative syndrome associated with abnormal lymphocyte apoptosis. Blood 89, 1341–1348 (1997).
  CAS PubMed Google Scholar
• Yang, X., Chang, H.Y. & Baltimore, D. Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell 1, 319–325 (1998).
  Article CAS PubMed Google Scholar
• Jaattela, M. & Tschopp, J. Caspase-independent cell death in T lymphocytes. Nat. Immunol. 4, 416–423.
• Holler, N. et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1, 489–495 (2000).
  Article CAS PubMed Google Scholar
• Li, M. & Beg, A.A. Induction of necrotic-like cell death by tumor necrosis factor-α and caspase inhibitors: novel mechanism for killing virus-infected cells. J. Virol. 74, 7470–7477 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Bertin, J. et al. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis. Proc. Natl. Acad. Sci. USA 94, 1172–1176 (1997).
  Article CAS PubMed PubMed Central Google Scholar
• Hu, S., Vincenz, C., Buller, M. & Dixit, V.M. A novel family of viral death effector domain-containing molecules that inhibit both CD95- and tumor necrosis factor receptor-1–induced apoptosis. J. Biol. Chem. 272, 9621–9624 (1997).
  Article CAS PubMed Google Scholar
• Thome, M. et al. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 386, 517–521 (1997).
  Article CAS PubMed Google Scholar
• Garvey, T.L., Bertin, J., Siegel, R.M., Lenardo, M.J. & Cohen, J. The death effector domains (DEDs) of the molluscum contagiosum virus MC159 v-FLIP protein are not functionally interchangeable with each other or with the DEDs of caspase-8. Virology 300, 217–225 (2002).
  Article CAS PubMed Google Scholar
• Irmler, M. et al. Inhibition of death receptor signals by cellular FLIP. Nature 388, 190–195 (1997).
  Article CAS PubMed Google Scholar
• Hu, S., Vincenz, C., Ni, J., Gentz, R. & Dixit, V.M. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1– and CD-95–induced apoptosis. J. Biol. Chem. 272, 17255–17257 (1997).
  Article CAS PubMed Google Scholar
• Kreuz, S., Siegmund, D., Scheurich, P. & Wajant, H. NF-κB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling. Mol. Cell. Biol. 21, 3964–3973 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Michaeu, O., Lens, S., Gaide, O., Alevizopoulos, K. & Tschopp, J. NF-κB signals induce the expression of c-FLIP. Mol. Cell. Biol. 21, 5299–5305 (2001).
  Article Google Scholar
• Thomas, R.K. et al. Constituitive expression of c-FLIP in Hodgkin and Reed-Sternberg cells. Amer. J. of Path. 160, 1521–1528 (2002).
  Article CAS Google Scholar
• Chang, D.W. et al. c-FLIPL is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. EMBO J. 21, 3704–3714 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Lens, S. et al. The caspase 8 inhibitor c-FLIPL modulates T-cell receptor–induced proliferation but not activation-induced cell death of lymphoctyes. Mol. Cell. Biol. 22, 5419–5433 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Condorelli, G. et al. PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis. Oncogene 18, 4409–4415 (1999).
  Article CAS PubMed Google Scholar
• Kitsberg, D. et al. Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNFα-induced apoptosis. J. Neuroscience 19, 8244–8251 (1999).
  Article CAS Google Scholar
• Araujo, H., Danziger, N., Cordier, J., Glowinski, J. & Chneiweiss, H. Characterization of PEA-15, a major substrate for protein kinase C in astrocytes. J. Biol. Chem. 268, 5911–5920 (1993).
  CAS PubMed Google Scholar
• Kubes, M., Cordier, J., Glowinski, J., Girault, J.A. & Chneiweiss, H. Endothelin induces a calcium-dependent phosphorylation of PEA-15 in intact astrocytes: identification of Ser104 and Ser116 phosphorylated, respectively, by protein kinase C and calcium/calmodulin kinase II in vitro. J. Neurochem. 71, 1307–1314 (1998).
  Article CAS PubMed Google Scholar
• Gomez-Angelats, M. & Cidlowski, J.A. Protein kinase C regulates FADD recruitment and death-inducing signaling complex formation in Fas/CD95-induced apoptosis. J. Biol. Chem. 276, 44944–44952 (2001).
  Article CAS PubMed Google Scholar
• Xiao, C., Yang, B.F., Asadi, N., Beguinot, F. & Hao, C. Tumor necrosis factor-related apoptosis-inducing ligand-induced death-inducing signaling complex and its modulation by c-FLIP and PED/PEA-15 in glioma cells. J. Biol. Chem. 277, 25020–25025 (2002).
  Article CAS PubMed Google Scholar
• Estelles, A., Charlton, C.A. & Blau, H.M. The phosphoprotein PEA-15 inhibits Fas- but increases TNF-R1 mediated caspase-8 activity and apoptosis. Dev. Biol. 216, 16–28 (1999).
  Article CAS PubMed Google Scholar
• Stegh, A.H. et al. DEDD, a novel death effector domain-containing protein, targeted to the nucleolus. EMBO J. 17, 5974–5986 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Schickling, O., Stegh, A.H., Byrd, J. & Peter, M.E. Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription. Cell Death Differ. 8, 1157–1161 (2001).
  Article CAS PubMed Google Scholar
• Lee, J. et al. DEDD regulates degradation of intermediate filaments during apoptosis. J. Cell. Biol. 158, 1051–1066 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Roth, W., Stenner-Liewen, F., Pawlowski, K., Godzik, A. & Reed, J.C. Identification and characterization of DEDD2, a death effector domain-containing protein. J. Biol. Chem. 277, 7501–7508 (2002).
  Article CAS PubMed Google Scholar
• Zheng, L., Schickling, O., Peter, M.E. & Lenardo, M.J. The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm. J. Biol. Chem. 276, 31945–31952 (2001).
  Article CAS PubMed Google Scholar
• Ng, F.W. et al. p28 Bap31, a Bcl-2/Bcl-XL– and procaspase-8–associated protein in the endoplasmic reticulum. J. Cell Biol. 139, 327–338 (1997).
  Article CAS PubMed PubMed Central Google Scholar
• Zhang, H. et al. BAR: an apoptosis regulator at the intersection of caspases and Bcl-2 family proteins. Proc. Natl. Acad. Sci. USA 97, 2597–2602 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Stegh, A.H. et al. Inactivation of caspase-8 on mitochondria of Bcl-xL-expressing MCF7-Fas cells: role for bifunctional apoptosis regulator protein. J. Biol. Chem. 277, 4351–4360 (2002).
  Article CAS PubMed Google Scholar
• Nguyen, M., Breckenridge, D.G., Ducret, A. & Shore, G.C. Caspase-resistant BAP31 inhibits Fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria. Mol. Cell. Biol. 20, 6731–6740 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Wang, B. et al. Uncleaved BAP31 in association with A4 protein at the endoplasmic reticulum is an inhibitor of Fas-initiated release of cytochrome c from mitochondria. J. Biol. Chem. advance online publication, 15 January 2003 (doi:10.1074/jbc.M209684200).
• Siegel, R.M. et al. Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis. J. Cell. Biol. 141, 1243–1253 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Zhang, J., Cado, D., Chen, A., Kabra, N.H. & Winoto, A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 392, 296–300 (1998).
  Article CAS PubMed Google Scholar
• Walsh, C.M. et al. A Role for FADD in T cell activation and development. Immunity 8, 439–449 (1998).
  Article CAS PubMed Google Scholar
• Newton, K., Harris, A.W., Bath, M.L., Smith, K.G. & Strasser, A. A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymhocytes. EMBO J. 17, 706–718 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Mack, A. & Hacker, G. Inhibition of caspase or FADD function blocks proliferation but not MAP kinase activation and interleukin-2 production during primary stimulation of T cells. Eur. J. Immunol. 32, 1986–1992 (2002).
  Article CAS PubMed Google Scholar
• Alam, A., Cohen, L.Y., Aouad, S. & Sekaly, R.P. Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells. J. Exp. Med. 190, 1879–1890 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Kennedy, N.J., Kataoka, T., Tschopp, J. & Budd, R.C. Caspase activation is required for T cell proliferation. J. Exp. Med. 190, 1891–1896 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Chun, H. et al. Pleiotropic lymphocyte activation defects due to caspase-8 mutation causes human immunodeficiency. Nature 419, 395–399 (2002).
  Article CAS PubMed Google Scholar
• Chaudhary, P.M. et al. Activation of the NF-κB pathway by caspase 8 and its homologs. Oncogene 19, 4451–4460 (2000).
  Article CAS PubMed Google Scholar
• Hu, W.H., Johnson, H. & Shu, H.B. Activation of NF-κB by FADD, Casper, and Caspase 8. J. Biol. Chem. 275, 10838–10844 (2000).
  Article CAS PubMed Google Scholar
• Wang, J. et al. Inherited caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell 98, 47–58 (1999).
  Article CAS PubMed Google Scholar
• Kataoka, T. et al. The caspase-8 inhibitor FLIP promotes activation of NF-κB and Erk signaling pathways. Curr. Biol. 10, 640–648 (2000).
  Article CAS PubMed Google Scholar
• Alderson, M.R. et al. Fas transduces activation signals in normal human T lymphocytes. J. Exp. Med. 178, 1891–1896 (1993).
  Google Scholar
• Ramos, J.W. et al. Death effector domain protein PEA-15 potentiates Ras activation of extracellular signal receptor-activated kinase by an adhesion-independent mechanism. Mol. Biol. Cell 11, 2863–2872 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Formstecher, E. et al. PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase. Dev. Cell 1, 239–250 (2001).
  Article CAS PubMed Google Scholar
• Ivanova, N.B. et al. A stem cell molecular signature. Science 298, 601–604 (2002).
  Article CAS PubMed Google Scholar
• Gervais, F.G. et al. Recruitment and activation of caspase-8 by the Huntington-interacting protein Hip-1 and a novel partner Hippi. Nat. Cell Biol. 4, 95–105 (2002).
  Article CAS PubMed Google Scholar