A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses

Nature Immunology

Volumn 8, Issue 5, 2007, Pages 497-503

  Mayor, Annick ^a   Martinon, Fabio ^a,c   De Smedt, Thibaut ^b   Pétrilli, Virginie ^a   Tschopp, Jürg ^a  

^a UNIVERSITY OF LAUSANNE   (Switzerland)

^b Apoxis SA   (Switzerland)

^c HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; HEAT SHOCK PROTEIN 90; I KAPPA B KINASE; PROTEIN SGT1; SMALL INTERFERING RNA; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CELL ACTIVITY; CONTROLLED STUDY; ENZYME ACTIVATION; HUMAN; HUMAN CELL; IMMUNOPATHOGENESIS; INFLAMMATORY DISEASE; INNATE IMMUNITY; MAMMAL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; TRANSCRIPTION INITIATION;

ANIMALS; CELL CYCLE PROTEINS; CELLS, CULTURED; HSP90 HEAT-SHOCK PROTEINS; HUMANS; IMMUNITY, NATURAL; INFLAMMATION; MICE; MICE, INBRED C57BL; NOD1 SIGNALING ADAPTOR PROTEIN; PLANT PROTEINS; PLANTS;

EID: 34247265509     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni1459     Document Type: Article

References (40)

1. Ogura, Y., Sutterwala, F.S. & Flavell, R.A. The inflammasome: First line of the immune response to cell stress. Cell 126, 659-662 (2006).
2. Martinon, F. & Tschopp, J. Inflammatory caspases and inflammasomes: master switches of inflammation. Cell Death Differ. 14, 10-22 (2007).
3. Martinon, F., Burns, K. & Tschopp, J. The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-1β. Mol. Cell 10, 417-426 (2002).
4. Hoffman, H.M., Mueller, J.L., Broide, D.H., Wanderer, A.A. & Kolodner, R.D. Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. Nat. Genet. 29, 301-305 (2001).
5. Hawkins, P.N., Lachmann, H.J., Aganna, E. & McDermott, M.F. Spectrum of clinical features in Muckle-Wells syndrome and response to anakinra. Arthritis Rheum. 50, 607-612 (2004).
6. Martinon, F., Agostini, L., Meylan, E. & Tschopp, J. Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome. Curr. Biol. 14, 1929-1934 (2004).
7. Kanneganti, T.D. et al. Bacterial RNA and small antiviral compounds activate caspase-1 through cryopyrin/Nalp3. Nature 440, 233-236 (2006).
8. Franchi, L. et al. Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in salmonella-infected macrophages. Nat. Immunol. 7, 576-582 (2006).
9. Miao, E.A. et al. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf. Nat. Immunol. 7, 569-575 (2006).
10. Martinon, F., Petrilli, V., Mayor, A., Tardivel, A. & Tschopp, J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440, 237-241 (2006).
11. Mariathasan, S. et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440, 228-232 (2006).
12. Sutterwala, F.S. et al. Critical role for NALP3/CIAS1/cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 24, 317-327 (2006).
13. Chae, J.J. et al. Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endotoxin and a defect in macrophage apoptosis. Mol. Cell 11, 591-604 (2003).
14. Chisholm, S.T., Coaker, G., Day, B. & Staskawicz, B.J. Host-microbe interactions: Shaping the evolution of the plant immune response. Cell 124, 803-814 (2006).
15. Jones, D.A. & Takemoto, D. Plant innate immunity - direct and indirect recognition of general and specific pathogen-associated molecules. Curr. Opin. Immunol. 16, 48-62 (2004).
16. Schulze-Lefert, P. Plant immunity: The origami of receptor activation. Curr. Biol. 14, R22-R24 (2004).
17. Holt, B.F., III, Hubert, D.A. & Dangl, J.L. Resistance gene signaling in plants-complex similarities to animal innate immunity. Curr. Opin. Immunol. 15, 20-25 (2003).
18. Meylan, E., Tschopp, J. & Karin, M. Intracellular pattern recognition receptors in the host response. Nature 442, 39-44 (2006).
19. Ting, J. & Davis, B. CATERPILLER: A novel gene family important in immunity, cell death, and diseases. Annu. Rev. Immunol. 23, 387-414 (2005).
20. Inohara, N., Chamaillard, M., McDonald, C. & Nunez, G. NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu. Rev. Biochem. 74, 355-383 (2005).
21. Sangster, T.A. & Queitsch, C. The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity. Curr. Opin. Plant Biol. 8, 86-92 (2005).
22. Shirasu, K. & Schulze-Lefert, P. Complex formation, promiscuity and multi-functionality: Protein interactions in disease-resistance pathways. Trends Plant Sci. 8, 252-258 (2003).
23. Azevedo, C. et al. The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance. Science 295 2073-2076 (2002).
24. Catlett, M.G. & Kaplan, K.B. Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p. J. Biol. Chem. 281, 33739-33748 (2006).
25. Takahashi, A., Casais, C., Ichimura, K. & Shirasu, K. HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. Proc. Natl. Acad. Sci. USA 100, 11777-11782 (2003).
26. Yao, F. et al. Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells. Hum. Gene Ther. 9 1939-1950 (1998).
27. O'Gorman, S., Fox, D.T. & Wahl, G.M. Recombinase-mediated gene activation and site-specific integration in mammalian cells. Science 251, 1351-1355 (1991).
28. Lu, R. et al. High throughput virus-induced gene silencing implicates heat shock protein 90 in plant disease resistance. EMBO J. 22, 5690-5699 (2003).
29. Holt, B.F., III, Belkhadir, Y. & Dangl, J.L. Antagonistic control of disease resistance protein stability in the plant immune system. Science 309, 929-932 (2005).
30. Hahn, J.S. Regulation of Nod1 by Hsp90 chaperone complex. FEBS Lett. 579, 4513-4519 (2005).
31. Inohara, N. et al. Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease. J. Biol. Chem. 278, 5509-5512 (2003).
32. Mariathasan, S. et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430, 213-218 (2004).
33. Zamboni, D.S. et al. The Birc1e cytosolic pattern-recognition receptor contributes to the detection and control of Legionella pneumophila infection. Nat. Immunol. 7, 318-325 (2006).
34. Pacey, S., Banerji, U., Judson, I. & Workman, P. Hsp90 inhibitors in the clinic. Handb. Exp. Pharmacol. 172, 331-358 (2006).
35. Lingelbach, L.B. & Kaplan, K.B. The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly. Mol. Cell. Biol. 24, 8938-8950 (2004).
36. Liu, Y., Burch-Smith, T., Schiff, M., Feng, S. & Dinesh-Kumar, S.P. Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants. J. Biol. Chem. 279, 2101-2108 (2004)
37. Sharp, S. & Workman, P. Inhibitors of the HSP90 molecular chaperone: current status. Adv. Cancer Res. 95, 323-348 (2006).
38. Niikura, Y. et al. 17-AAG, an Hsp90 inhibitor, causes kinetochore defects: A novel mechanism by which 17-AAG inhibits cell proliferation. Oncogene 25, 4133-4146 (2006).
39. Agostini, L. et al. NALP3 forms an IL-1β processing inflammasome with increased activity in Muckle-Wells auto-inflammatory disorder. Immunity 20, 319-325 (2004).
40. Thome, M. et al. Identification of CARDIAK, a RIP-like kinase that associates with caspase-1. Curr. Biol. 8, 885-888 (1998).