IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL- 1 signaling

Science

Volumn 278, Issue 5343, 1997, Pages 1612-1615

  Muzio, Marta ^a,c   Ni, Jian ^b   Feng, Ping ^b   Dixit, Vishva M ^a,d  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b GLAXOSMITHKLINE   (United States)

^c MARIO NEGRI INSTITUTE FOR PHARMACOLOGICAL RESEARCH   (Italy)

^d GENENTECH INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN;

ADAPTATION; ARTICLE; DROSOPHILA; ENZYME ACTIVATION; ENZYME ACTIVITY; MEDIATOR RELEASE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FAMILY; SEQUENCE HOMOLOGY;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; ANTIGENS, DIFFERENTIATION; CARRIER PROTEINS; CELL LINE; DROSOPHILA PROTEINS; HUMANS; INTERLEUKIN-1; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASES; MOLECULAR SEQUENCE DATA; MYELOID DIFFERENTIATION FACTOR 88; NF-KAPPA B; PROTEIN KINASES; PROTEIN-SERINE-THREONINE KINASES; PROTEINS; RECEPTORS, IMMUNOLOGIC; RECEPTORS, INTERLEUKIN-1; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; TNF RECEPTOR-ASSOCIATED FACTOR 6; TRANSFECTION;

MAMMALIA;

EID: 0030694108     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5343.1612     Document Type: Article

References (30)

1. S. A. Greenfeder et al., J. Biol. Chem. 270, 13757 (1995).
2. J. E. Sims et al., Science 241, 585 (1988).
3. C. Korherr, R. Hofmeister, H. Wesche, W. Falk, Eur. J. Immunol. 27, 262 (1997).
4. H. Wesche et al., J. Biol. Chem. 272, 7727 (1997).
5. N. W. Freshney et al., Cell 78, 1039 (1994).
6. M. Martin, G. F. Bol, A. Eriksson, K. Resch, R. Brigelius-Flohe, Eur. J. Immunol. 24, 1566 (1994).
7. R. L. Galindo, D. N. Edwards, S. K. Gillespie, S. A. Wasserman, Development 121, 2209 (1995).
8. J. L. Norris and J. L. Manley, Genes Dev. 10, 862 (1996).
9. A. Letsou, S. Alexander, A. Wasserman, EMBO J. 12, 3449 (1993).
10. J. Grosshans, A. Bergmann, P. Haffter, C. Nusslein-Volhard, Nature 372, 563 (1994).
11. Z. Cao, W. J. Henzel, X. Gao, Science 271, 1128 (1996).
12. A. Eriksson, G. D. Bird, S. K. Dower, Cytokine 7, 649 (1995).
13. R. Singh, T. Guth, M. Konieczkowski, R. Sedor, J. Clin. Invest. 100, 419 (1997).
14. H. Duan and V. Dixit, Nature 385, 86 (1997).
15. M. Tewari et al., Cell 81, 801 (1995).
16. N. L. Malinin, M. P. Boldin, A. V. Kovalenko, D. Wallach, Nature 385, 540 (1997).
17. Z. Cao, J. Xiong, M. Takeuchi, T. Kurama, D. Goeddel, ibid. 383, 443 (1996).
18. K. Lord, B. Hoffman-Liebermann, D. A. Liebermann, Oncogene 5, 1095 (1990).
19. E. Feinstein, A. Kimchi, D. Wallach, M. Boldin, E. Varfolomeev, Trends Biochem. Sci. 20, 342 (1995).
20. K. Hofmann and J. Tschopp, FEBS Lett. 371, 321 (1995).
21. D. Hultmark, Biochem. Biophys. Res. Commun. 199, 144 (1994).
22. G. Hardiman, F. L. Rock, S. Balasubramanian, R. A. Kastelein, J. F. Bazan, Oncogene 13, 2467 (1996).
23. T. Bonnert et al., FEBS Lett. 402, 81 (1997).
24. R. Medzhitov, P. Preston-Hurlburt, C. A. Janeway Jr., Nature 388, 394 (1997).
25. A. Chinnaiyan, K. O'Rourke, M. Tewari, V. Dixit, Cell 81, 505 (1995).
26. S. K. Hanks, A. M. Quinn, T. Hunter, Science 241, 42 (1988).
27. In the NF-κB luciferase assay, cells were transfected with ELAM-Luciferase reporter plasmid (0.1 μg), pCMV-β-galactosidase (β-Gal) (0.2 μg), and the indicated expression vectors; the total amount of transfected DNA was kept constant by supplementation with empty vector. Relative NF-κB activity was calculated by normalizing relative luciferase activity with β-Gal activity as previously described (77). Data shown are from one out of three to six independent experiments with similar qualitative results. Data from experiments performed in duplicate or triplicate are expressed as mean ± SE.
28. G. Croston, Z. Cao, D. V. Goeddel, J. Biol. Chem. 270, 16514 (1995).
29. Transfection and coimmunoprecipitation were done as follows. Human embryonic 293 or 293T cells were transiently transfected by the calcium phosphate method with the indicated plasmids. The total amount of DNA was kept constant. Twenty-four to 36 hours after transfection, cells were lysed in 0.5 ml of buffer (1% NP-40, 150 mM NaCl, 50 mM tris, 1 mM EDTA, and protease inhibitors cocktail). Cell lysates were adjusted to 0.7 M NaCl, and the indicated antibodies were added for 1 to 4 hours. Immune complexes were precipitated by the addition of protein G-Sepharose (Sigma). After extensive washing, the Sepharose beads were boiled in sample buffer and the eluted proteins were fractionated by SDS-polyacrylamide gel electrophoresis. Subsequent immunoblotting was performed as described (25).
30. M.M. is supported by a Human Frontier Science Program Organization fellowship. We thank Z. Cao for helpful discussions and reagents; I. Jones for help with figures; and D. Chaudhary, A. Chinnaiyan, H. Duan, S. Hu, E. Humke, J. McCarthy, K. O'Rourke, G. Pan, and C. Vincenz for encouragement and discussions.