Signal transduction by DR3, a death domain-containing receptor related to TNFR-1 and CD95

Science

Volumn 274, Issue 5289, 1996, Pages 990-992

  Chinnaiyan, Arul M ^a   O'Rourke, Karen ^a   Yu, Guo Liang ^b   Lyons, Robert H ^a   Garg, Manish ^a   Duan, D Roxanne ^b   Xing, Lily ^b   Gentz, Reiner ^b   Ni, Jian ^b   Dixit, Vishva M ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b GLAXOSMITHKLINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DISEASES; DNA SEQUENCES; ENZYMES; GENES; MOLECULES; TISSUE;

AMINO ACID SEQUENCE; APOPTOSIS; CYTOKINE RECEPTORS; GLYCOSYLATION; HOMEOSTASIS; INTRACELLULAR HOMOLOGY; LYMPHOCYTES; NERVE GROWTH FACTOR RECEPTOR; SIGNAL TRANSDUCTION; TUMOR NECROSIS FACTOR RECEPTOR;

CELLS;

CYTOKINE RECEPTOR; FAS ANTIGEN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR;

AMINO ACID SEQUENCE; APOPTOSIS; ARTICLE; CELL DEATH; CONTROLLED STUDY; HOMEOSTASIS; HUMAN; HUMAN TISSUE; LYMPHOCYTE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; ANTIGENS, CD95; APOPTOSIS; CARRIER PROTEINS; CASPASE 8; CASPASE 9; CASPASES; CLONING, MOLECULAR; CYSTEINE ENDOPEPTIDASES; FAS-ASSOCIATED DEATH DOMAIN PROTEIN; GENE LIBRARY; HUMANS; LYMPHOCYTES; MOLECULAR SEQUENCE DATA; NF-KAPPA B; ORGAN SPECIFICITY; PROTEINS; RECEPTORS, TUMOR NECROSIS FACTOR; RECEPTORS, TUMOR NECROSIS FACTOR, MEMBER 25; RNA, MESSENGER; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; TNF RECEPTOR-ASSOCIATED FACTOR 1; TNF RECEPTOR-ASSOCIATED FACTOR 2; TRANSFECTION; TUMOR CELLS, CULTURED;

EID: 10544236916     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5289.990     Document Type: Article

References (36)

1. H. Steller, Science 267, 1445 (1995).
2. C. B. Thompson, ibid., p. 1456.
3. J. L. Cleveland and J. N. Ihle, Cell 81, 479 (1995); A. Fraser and G. Evan, ibid. 85, 781 (1996); S. Nagata and P. Golstein, Science 267, 1449 (1995).
4. J. L. Cleveland and J. N. Ihle, Cell 81, 479 (1995); A. Fraser and G. Evan, ibid. 85, 781 (1996); S. Nagata and P. Golstein, Science 267, 1449 (1995).
5. J. L. Cleveland and J. N. Ihle, Cell 81, 479 (1995); A. Fraser and G. Evan, ibid. 85, 781 (1996); S. Nagata and P. Golstein, Science 267, 1449 (1995).
6. C. A. Smith et al., Science 248, 1019 (1990).
7. P. Golstein, D. Marguet, V. Depraetere, Cell 81, 185 (1995); K. White et al., Science 264, 677 (1994).
8. P. Golstein, D. Marguet, V. Depraetere, Cell 81, 185 (1995); K. White et al., Science 264, 677 (1994).
9. A. M. Chinnaiyan, K. O'Rourke, M. Tewari, V. M. Dixit, Cell 81, 505 (1995); M. P. Boldin et al., J. Biol. Chem. 270, 7795 (1995); F. C. Kischkel et al., EMBO J. 14, 5579 (1995).
10. A. M. Chinnaiyan, K. O'Rourke, M. Tewari, V. M. Dixit, Cell 81, 505 (1995); M. P. Boldin et al., J. Biol. Chem. 270, 7795 (1995); F. C. Kischkel et al., EMBO J. 14, 5579 (1995).
11. A. M. Chinnaiyan, K. O'Rourke, M. Tewari, V. M. Dixit, Cell 81, 505 (1995); M. P. Boldin et al., J. Biol. Chem. 270, 7795 (1995); F. C. Kischkel et al., EMBO J. 14, 5579 (1995).
12. M. Muzio et al., Cell 85, 817 (1996); M. P. Boldin, T. M. Goncharov, Y. V. Goltsev, D. Wallach, ibid., p. 803.
13. M. Muzio et al., Cell 85, 817 (1996); M. P. Boldin, T. M. Goncharov, Y. V. Goltsev, D. Wallach, ibid., p. 803.
14. L. A. Tartaglia and D. V. Goeddel, Immunol. Today 13, 151 (1992).
15. H. Hsu, J. Xiong, D. V. Goeddel, Cell 81, 495 (1995).
16. H. Hsu, H.-B. Shu, M.-P. Pan, D. V. Goeddel, ibid. 84, 299 (1996).
17. H. Hsu, J. Huang, H.-B. Shu, V. Baichwal, D. V. Goeddel, Immunity 4, 387 (1996).
18. M. D. Adams et al., Nature 377 (suppl.), 3 (1995); G. S. Feng et al., J. Biol. Chem. 271, 12129 (1996).
19. M. D. Adams et al., Nature 377 (suppl.), 3 (1995); G. S. Feng et al., J. Biol. Chem. 271, 12129 (1996).
20. R. Watanabe-Fukunaga et al., J. Immunol. 148, 1274 (1992).
21. M. Rothe, S. C. Wong, W. J. Henzel, D. V. Goeddel, Cell 78, 681 (1994); M. Rothe, V. Sarma, V. M. Dixit, D. V. Goeddel, Science 269, 1424 (1995).
22. M. Rothe, S. C. Wong, W. J. Henzel, D. V. Goeddel, Cell 78, 681 (1994); M. Rothe, V. Sarma, V. M. Dixit, D. V. Goeddel, Science 269, 1424 (1995).
23. B. Z. Stanger, P. Leder, T. H. Lee, E. Kim, B. Seed, Cell 81, 513 (1995).
24. A. M. Chinnaiyan, K. O'Rourke, V. M. Dixit, unpublished data.
25. M. Tewari and V. M. Dixit, J. Biol. Chem. 270, 3255 (1995).
26. A. M. Chinnaiyan et al., ibid. 271, 4961 (1996).
27. R. Pitti et al., ibid., p. 12687; S. R. Wiley et al., Immunity 3, 673 (1995).
28. R. Pitti et al., ibid., p. 12687; S. R. Wiley et al., Immunity 3, 673 (1995).
29. S. A. Marsters et al., Curr. Biol. 6, 750 (1996).
30. R. Watanabe-Fukunaga, C. I. Brannan, N. G. Copeland, N. A. Jenkins, S. Nagata, Nature 356, 314 (1992); N. Itoh and S. Nagata, J. Biol. Chem. 268, 10932 (1993).
31. R. Watanabe-Fukunaga, C. I. Brannan, N. G. Copeland, N. A. Jenkins, S. Nagata, Nature 356, 314 (1992); N. Itoh and S. Nagata, J. Biol. Chem. 268, 10932 (1993).
32. In vitro binding experiments were done as described in (6).
33. The constructs encoding Flag-TNFR-1 and Flag-ΔTNFR-1 were described elsewhere (18). To facilitate epitope tagging, we cloned DR3 and ΔDR3(1-321) into the FLAG plasmid pCMV1FLAG (IBI Kodak) with the use of the signal peptide provided by the vector. Transfection of 293 cells was done by calcium phosphate precipitation with the constructs encoding the indicated proteins in combination with pcDNA3-CrmA (17) to prevent cell death and thus maintain protein expression. Cells were lysed in 1 ml of lysis buffer (50 mM Hepes, 150 mM NaCl, 1 mM EDTA, 1% NP-40, and a protease inhibitor cocktail). Lysates were immunoprecipitated with a control monoclonal antibody (mAb) or Flag mAb for at least 4 hours at 4°C, as described (18). The beads were washed three times with lysis buffer, but in the case of TRADD binding, the NaCl concentration was adjusted to 1 M. The precipitates were fractionated by 12.5% SDS-polyacrylamide gel electrophoresis (PAGE) and transferred to nitrocellulose. Subsequent protein immunoblotting was performed as described (10, 18).
34. Cell death assays were done as described (6, 18). The data (mean ± SD) are the percentage of round blue cells among the total number of blue cells counted. Data were obtained from at least three independent experiments.
35. NF-κB luciferase assays were performed as described (11, 12, 14, 18). The amounts of dominant negative inhibitors used were four times the amounts of the death receptors. Total DNA was kept constant.
36. Supported by the Medical Scientist Training Program (A.M.C.) and NIH grant GM-07863 (A.M.C.). The initial EST clones used in this study were discovered as part of a joint collaboration between scientists at The Institute for Genomic Research and at Human Genome Sciences. We thank D. Goeddel for the TRAF2 and RIP constructs, I. Jones for manuscript preparation, and H. Duan and C. Vincenz for helpful discussions.