Function of GRIM-19, a mitochondrial respiratory chain complex I protein, in innate immunity

Journal of Biological Chemistry

Volumn 287, Issue 32, 2012, Pages 27227-27235

  Chen, Yong ^b,c   Lu, Hao ^b   Liu, Qian ^a   Huang, Guochang ^b,d   Lim, Cheh Peng ^b,e   Zhang, Lianhui ^b   Hao, Aijun ^a   Cao, Xinmin ^a,b  

^a SHANDONG UNIVERSITY   (China)

^b INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Singapore)

^c KK WOMEN'S AND CHILDREN'S HOSPITAL   (Singapore)

^d MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^e NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL CHALLENGE; BACTERIAL INFECTIONS; CELLULAR ENERGY; CYTOKINE PRODUCTION; ENGULFMENT; IN-VIVO; INFLAMMATORY RESPONSE; INNATE IMMUNITY; INTERLEUKIN1; KNOCK OUTS; LIPOPOLYSACCHARIDES; MITOCHONDRIAL COMPLEX; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL RESPIRATORY CHAIN; MONODANSYLCADAVERINE; MULTISUBUNIT COMPLEXES; PROINFLAMMATORY CYTOKINES; REACTIVE OXYGEN SPECIES; RESPIRATORY CHAINS; UP-REGULATION; URINARY TRACT INFECTIONS; WILD TYPES;

BACTERIA; CELL DEATH; MACROPHAGES; MAMMALS; OXYGEN; PROTEINS;

MITOCHONDRIA;

CYTOKINE; DANSYLCADAVERINE; GAMMA INTERFERON; GRIM 19 PROTEIN; INTERLEUKIN 1; INTERLEUKIN 12; INTERLEUKIN 6; LIPOPOLYSACCHARIDE; PROTEIN; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; BACTERIAL INFECTION; BACTERICIDAL ACTIVITY; CELL ENERGY; CYTOKINE PRODUCTION; ENERGY YIELD; FEMALE; IN VIVO STUDY; INFLAMMATION; INNATE IMMUNITY; INTRACELLULAR KILLING; LYSOSOME; MACROPHAGE; MALE; MITOCHONDRIAL RESPIRATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN SUBUNIT; STAPHYLOCOCCUS SAPROPHYTICUS; UPREGULATION; URINARY TRACT INFECTION; WILD TYPE;

ANIMALS; APOPTOSIS REGULATORY PROTEINS; ELECTRON TRANSPORT COMPLEX I; FEMALE; HUMANS; IMMUNITY, INNATE; MICE; NADH, NADPH OXIDOREDUCTASES;

BACTERIA (MICROORGANISMS); MUS; STAPHYLOCOCCUS SAPROPHYTICUS;

EID: 84864540360     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.340315     Document Type: Article

References (34)

1. West, A. P., Shadel, G. S., and Ghosh, S. (2011) Mitochondria in innate immune responses. Nat. Rev. Immunol. 11, 389-402
2. Scott, I. (2010) The role of mitochondria in the mammalian antiviral defense system. Mitochondrion 10, 316-320
3. Newmeyer, D. D., and Ferguson-Miller, S. (2003) Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112, 481-490 (Pubitemid 36263081)
4. Hatefi, Y. (1985) The mitochondrial electron transport and oxidative phosphorylation system. Annu. Rev. Biochem. 54, 1015-1069
5. Schultz, B. E., and Chan, S. I. (2001) Structures and proton-pumping strategies of mitochondrial respiratory enzymes. Annu. Rev. Biophys. Biomol. Struct. 30, 23-65 (Pubitemid 32566155)
6. Boveris, A., and Chance, B. (1973) The mitochondrial generation of hydrogen peroxide: general properties and effect of hyperbaric oxygen. Biochem. J. 134, 707-716
7. Melov, S., Coskun, P. E., and Wallace, D. C. (1999) Mouse models of mitochondrial disease, oxidative stress, and senescence. Mutat. Res. 434, 233-242 (Pubitemid 29352258)
8. Danial, N. N., and Korsmeyer, S. J. (2004) Cell death: critical control points. Cell 116, 205-219 (Pubitemid 38167313)
9. Cao, X., and Chen, Y. (2009) Mitochondria and calcium signaling in embryonic development. Semin. Cell Dev. Biol. 20, 337-345
10. Angell, J. E., Lindner, D. J., Shapiro, P. S., Hofmann, E. R., and Kalvakolanu, D. V. (2000) Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-β and retinoic acid combination, using a genetic approach. J. Biol. Chem. 275, 33416-33426
11. Fearnley, I. M., Carroll, J., Shannon, R. J., Runswick, M. J., Walker, J. E., and Hirst, J. (2001) GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 276, 38345-38348
12. Huang, G., Lu, H., Hao, A., Ng, D. C., Ponniah, S., Guo, K., Lufei, C., Zeng, Q., and Cao, X. (2004) GRIM-19, a cell death regulatory protein, is essential for assembly and function of mitochondrial complex I. Mol. Cell. Biol. 24, 8447-8456 (Pubitemid 39245067)
13. Lu, H., and Cao, X. (2008) GRIM-19 is essential for maintenance of mitochondrial membrane potential. Mol. Biol. Cell 19, 1893-1902
14. Carroll, J., Fearnley, I. M., Skehel, J. M., Shannon, R. J., Hirst, J., and Walker, J. E. (2006) Bovine complex I is a complex of 45 different subunits. J. Biol. Chem. 281, 32724-32727 (Pubitemid 46036828)
15. Chen, Y., Yuen, W. H., Fu, J., Huang, G., Melendez, A. J., Ibrahim, F. B., Lu, H., and Cao, X. (2007) The mitochondrial respiratory chain controls intracellular calcium signaling and NFAT activity essential for heart formation in Xenopus laevis. Mol. Cell. Biol. 27, 6420-6432 (Pubitemid 47435748)
16. Raz, R., Colodner, R., and Kunin, C. M. (2005) Who are you-Staphylococcus saprophyticus? Clin. Infect. Dis. 40, 896-898
17. Høyer-Hansen, M., Bastholm, L., Mathiasen, I. S., Elling, F., and Jäättelä, M. (2005) Vitamin D analog EB1089 triggers dramatic lysosomal changes and Beclin 1-mediated autophagic cell death. Cell Death Differ. 12, 1297-1309
18. Herskovits, A. A., Auerbuch, V., and Portnoy, D. A. (2007) Bacterial ligands generated in a phagosome are targets of the cytosolic innate immune system. PLoS Pathog. 3, e51
19. Smeitink, J. A., Zeviani, M., Turnbull, D. M., and Jacobs, H. T. (2006) Mitochondrial medicine: a metabolic perspective on the pathology of oxidative phosphorylation disorders. Cell Metab. 3, 9-13
20. Wallace, D. C. (1999) Mitochondrial diseases in man and mouse. Science 283, 1482-1488
21. Moore, C. B., Bergstralh, D. T., Duncan, J. A., Lei, Y., Morrison, T. E., Zimmermann, A. G., Accavitti-Loper, M. A., Madden, V. J., Sun, L., Ye, Z., Lich, J. D., Heise, M. T., Chen, Z., and Ting, J. P. (2008) NLRX1 is a regulator of mitochondrial antiviral immunity. Nature 451, 573-577 (Pubitemid 351186265)
22. Seth, R. B., Sun, L., Ea, C. K., and Chen, Z. J. (2005) Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF 3. Cell 122, 669-682 (Pubitemid 41242633)
23. Tattoli, I., Carneiro, L. A., Jéhanno, M., Magalhaes, J. G., Shu, Y., Philpott, D. J., Arnoult, D., and Girardin, S. E. (2008) NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-κB and JNK pathways by inducing reactive oxygen species production. EMBO Rep. 9, 293-300 (Pubitemid 351330996)
24. Arnoult, D., Soares, F., Tattoli, I., Castanier, C., Philpott, D. J., and Girardin, S. E. (2009) An N-terminal addressing sequence targets NLRX1 to the mitochondrial matrix. J. Cell Sci. 122, 3161-3168
25. Castanier, C., Garcin, D., Vazquez, A., and Arnoult, D. (2010) Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway. EMBO Rep. 11, 133-138
26. Klionsky, D. J., and Emr, S. D. (2000) Autophagy as a regulated pathway of cellular degradation. Science 290, 1717-1721 (Pubitemid 32004796)
27. Nakagawa, I., Amano, A., Mizushima, N., Yamamoto, A., Yamaguchi, H., Kamimoto, T., Nara, A., Funao, J., Nakata, M., Tsuda, K., Hamada, S., and Yoshimori, T. (2004) Autophagy defends cells against invading group A Streptococcus. Science 306, 1037-1040 (Pubitemid 39482907)
28. Gutierrez, M. G., Master, S. S., Singh, S. B., Taylor, G. A., Colombo, M. I., and Deretic, V. (2004) Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119, 753-766 (Pubitemid 40017683)
29. Ogawa, M., Yoshimori, T., Suzuki, T., Sagara, H., Mizushima, N., and Sasakawa, C. (2005) Escape of intracellular Shigella from autophagy. Science 307, 727-731 (Pubitemid 40194643)
30. Wallace, D. C. (2005) Mitochondria and cancer: Warburg addressed. Cold Spring Harbor Symp. Quant. Biol. 70, 363-374
31. Hoetzenecker, W., Echtenacher, B., Guenova, E., Hoetzenecker, K., Woelbing, F., Brück, J., Teske, A., Valtcheva, N., Fuchs, K., Kneilling, M., Park, J. H., Kim, K. H., Kim, K. W., Hoffmann, P., Krenn, C., Hai, T., Ghoreschi, K., Biedermann, T., and Röcken, M. (2012) ROS-induced ATF3 causes susceptibility to secondary infections during sepsis-associated immunosuppression. Nat. Med. 18, 128-134
32. Jendrysik, M. A., Vasilevsky, S., Yi, L., Wood, A., Zhu, N., Zhao, Y., Koontz, S. M., and Jackson, S. H. (2011) NADPH oxidase-2-derived ROS dictates murine DC cytokine-mediated cell fate decisions during CD4 T helper-cell commitment. PloS One 6, e28198
33. Khan, N., Rahim, S. S., Boddupalli, C. S., Ghousunnissa, S., Padma, S., Pathak, N., Thiagarajan, D., Hasnain, S. E., and Mukhopadhyay, S. (2006) Hydrogen peroxide inhibits IL-12 p40 induction in macrophages by inhibiting c-rel translocation to the nucleus through activation of calmodulin protein. Blood 107, 1513-1520 (Pubitemid 43242389)
34. Barnich, N., Hisamatsu, T., Aguirre, J. E., Xavier, R., Reinecker, H. C., and Podolsky, D. K. (2005) GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of antibacterial function in intestinal epithelial cells. J. Biol. Chem. 280, 19021-19026 (Pubitemid 41379607)