Molecular mechanisms of mitochondrial DNA release and activation of the cGAS-STING pathway

참고문헌 (115)

1. Ishikawa, H., "STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling", Nature, 455, pp.674~678 (2008)
2. Andreeva, L., "cGAS senses long and HMGB", TFAM-bound U-turn DNA by forming protein-DNA ladders, 2017, pp.549, 394~398
3. Civril, F., "Structural mechanism of cytosolic DNA sensing by cGAS", Nature, 498, pp.332~337 (2013)
4. West, A. P., "Mitochondria in innate immune responses", Nat. Rev. Immunol, 11, pp.389~402 (2011)
5. Takeuchi, O., "Pattern recognition receptors and inflammation", Cell, 140, pp.805~820 (2010)
6. Ning, X., "Apoptotic caspases suppress type I interferon production via the cleavage of cGAS, MAVS, and IRF3", Mol. Cell, 74, pp.19~31 (2019)
7. Liu, S., "Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation", Science, 347, pp.aaa2630~ (2015)
8. Zhou, R., "A role for mitochondria in NLRP3inflammasome activation", Nature, 469, pp.221~225 (2011)
9. Wang, Y., "Inflammasome activation triggers caspase-1-mediated cleavage of cGAS to regulate responses to DNA virus infection", Immunity, 46, pp.393~404 (2017)
10. Shimada, K., "Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis", Immunity, 36, pp.401~414 (2012)
11. Zhong, Z., "New mitochondrial DNA synthesis enables NLRP3 inflammasome activation", Nature, 560, pp.198~203 (2018)
12. is the metazoan second messenger produced by DNA-activated cyclic GMP-AMP synthase, "Cell", 2013, 1094~1107
13. Herzner, A. M., "Sequence-specific activation of the DNA sensor cGAS by Y-form DNA structures as found in primary HIV-1 cDNA", Nat. Immunol, 16, pp.1025~1033 (2015)
14. Zhang, C., "Structural basis of STING binding with and phosphorylation by TBK1", Nature, 567, pp.394~398 (2019)
15. Sun, L., "Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway", Science, 339, pp.786~791 (2013)
16. Shoshan-Barmatz, V., "Apoptosis is regulated by the VDAC1 N-terminal region and by VDAC oligomerization : release of cytochrome c, AIF and Smac", Diablo, 2010, pp.1797, 1281~1291
17. West, A. P., "Mitochondrial DNA stress primes the antiviral innate immune response", Nature, 520, pp.553~557 (2015)
18. Sun, W., "ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization", Proc. Natl Acad. Sci. USA, 106, pp.8653~8658 (2009)
19. Zhong, B., "The adaptor protein MITA links virus-sensing receptors to IRF3transcription factor activation", Immunity, 29, pp.538~550 (2008)
20. Woodward, J. J., "c-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response", Science, 328, pp.1703~1705 (2010)
21. Li, X. D., "Pivotal roles of cGAS-cGAMP signaling in antiviral defense and immune adjuvant effects", Science, 341, pp.1390~1394 (2013)
22. Li, X., "Cyclic GMP-AMP synthase is activated by double-stranded DNAinduced ligomerization", Immunity, 39, pp.1019~1031 (2013)
23. Ablasser, A., "cGAS produces a 2’-5’-linked cyclic dinucleotide second messenger that activates STING", Nature, 498, pp.380~384 (2013)
24. Kranzusch, P. J., "Structure of human cGAS reveals a conserved family of second-messenger enzymes in innate immunity", Cell Rep, 3, pp.1362~1368 (2013)
25. Lahaye, X., "NONO detects the nuclear HIV capsid to promote cGASmediated innate immune activation", Cell, 175, pp.488~501 (2018)
26. Barnett, K. C., "Phosphoinositide interactions position cGAS at the plasma membrane to ensure efficient distinction between self-and viral DNA", Cell, 176, pp.1432~1446 (2019)
27. Mankan, A. K., "Cytosolic RNA : DNA hybrids activate the cGAS-STING axis", EMBO J, 33, pp.2937~2946 (2014)
28. Luecke, S., "cGAS is activated by DNA in a length-dependent manner", EMBO Rep, 18, pp.1707~1715 (2017)
29. Xie, W., "Human cGAS catalytic domain has an additional DNA-binding interface that enhances enzymatic activity and liquid-phase condensation", Proc. Natl. Acad. Sci. USA, 116, pp.11946~11955 (2019)
30. Du, M, "DNA-induced liquid phase condensation of cGAS activates innate immune signaling", Science, 361, pp.704~709 (2018)
31. Seo, G. J., "Akt kinase-mediated checkpoint of cGAS DNA sensing pathway", Cell Rep, 13, pp.440~449 (2015)
32. Sun, X., "DNA-PK deficiency potentiates cGAS-mediated antiviral innate immunity", Nat. Commun, 11, pp.6182~ (2020)
33. Li, T., "Phosphorylation and chromatin tethering prevent cGAS activation during mitosis", Science, 371, pp.eabc5386~ (2021)
34. Li, M., "Dephosphorylation of cGAS by PPP6C impairs its substrate binding activity and innate antiviral response", Protein Cell, 11, pp.584~599 (2020)
35. Xia, P., "Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity", Nat. Immunol, 17, pp.369~378 (2016)
36. Hu, M. M., "Sumoylation promotes the stability of the DNA sensor cGAS and the adaptor STING to regulate the kinetics of response to DNA virus", Immunity, 45, pp.555~569 (2016)
37. Wang, Q., "The E3 ubiquitin ligase RNF185 facilitates the cGAS-mediated innate immune response", PLoS Pathog, 13, pp.e1006264~ (2017)
38. Chen, M., "TRIM14 inhibits cGAS degradation mediated by selective autophagy receptor p62 to promote innate immune responses", Mol. Cell, 64, pp.105~119 (2016)
39. Ohkuri, T., "Intratumoral administration of cGAMP transiently accumulates potent macrophages for anti-tumor immunity at a mouse tumor site", Cancer Immunol. Immunother, 66, pp.705~716 (2017)
40. Li, T., "Antitumor activity of cGAMP via stimulation of cGAS-cGAMP-STINGIRF3mediated innate immune response", Sci. Rep, 6, pp.19049~ (2016)
41. Dorostkar, F., "Co-administration of 2'3’-cGAMP STING activator and CpG-C adjuvants with a mutated form of HPV 16 E7 protein leads to tumor growth inhibition in the mouse model", Infect. Agent. Cancer, 16, pp.7~ (2021)
42. Carozza, J. A., "Extracellular cGAMP is a cancer cell-produced immunotransmitter involved in radiation-induced anti-cancer immunity", Nat. Cancer, 1, pp.184~196 (2020)
43. Kato, K., "Structural insights into cGAMP degradation by Ecto-nucleotide pyrophosphatase phosphodiesterase 1", Nat. Commun, 9, pp.4424~ (2018)
44. Carozza, J. A., "ENPP1’s regulation of extracellular cGAMP is a ubiquitous mechanism of attenuating STING signaling", Proc. Natl Acad. Sci. USA, 119, pp.e2119189119~ (2022)
45. Ritchie, C., "SLC19A1 is an importer of the immunotransmitter cGAMP", Mol. Cell, 75, pp.372~381 (2019)
46. Luteijn, R. D., "SLC19A1 transports immunoreactive cyclic dinucleotides", Nature, 573, pp.434~438 (2019)
47. Zhou, Y., "Blockade of the phagocytic receptor MerTK on tumor-associated macrophages enhances P2X7R-dependent STING activation by tumor-derived cGAMP", Immunity, 52, pp.357~373 (2020)
48. Drill, M., "Inhibition of purinergic P2X receptor 7(P2X7R)decreases granulocyte-macrophage colony-stimulating factor(GM-CSF)expression in U251 glioblastoma cells", Sci. Rep, 10, pp.14844~ (2020)
49. Zhou, C., "Transfer of cGAMP into bystander cells via LRRC8 volumeregulated anion channels augments STING-mediated interferon responses and anti-viral immunity", Immunity, 52, pp.767~781 (2020)
50. Xie, Y., "Gut epithelial TSC1", mTOR controls RIPK3-dependent necroptosis in intestinal inflammation and cancer, 2020, pp.130, 2111~2128
51. Li, X., "An alternatively spliced STING isoform localizes in the cytoplasmic membrane and directly senses extracellular cGAMP", J. Clin. Invest, 132, pp.e144339~ (2022)
52. Ablasser, A., "Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP", Nature, 503, pp.530~534 (2013)
53. Kalamvoki, M., "Cells infected with herpes simplex virus 1export to uninfected cells exosomes containing STING, viral mRNAs, and microRNAs", Proc. Natl. Acad. Sci. USA, 111, pp.E4991~E4996 (2014)
54. Bridgeman, A., "Viruses transfer the antiviral second messenger cGAMP between cells", Science, 349, pp.1228~1232 (2015)
55. Liu, H., "cGAS facilitates sensing of extracellular cyclic dinucleotides to activate innate immunity", EMBO Rep, 20, pp.e46293~ (2019)
56. Shang, G., "Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP", Nature, 567, pp.389~393 (2019)
57. Yin, Q., "Cyclic di-GMP sensing via the innate immune signaling protein STING", Mol. Cell, 46, pp.735~745 (2012)
58. Ouyang, S., "Structural analysis of the STING adaptor protein reveals a hydrophobic dimer interface and mode of cyclic di-GMP binding", Immunity, 36, pp.1073~1086 (2012)
59. Huang, Y. H., "The structural basis for the sensing and binding of cyclic di-GMP by STING", Nat. Struct. Mol. Biol, 19, pp.728~730 (2012)
60. Shang, G., "Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP", Nat. Struct. Mol. Biol, 19, pp.725~727 (2012)
61. Ergun, S. L., "STING polymer structure reveals mechanisms for activation, hyperactivation, and inhibition", Cell, 178, pp.290~301 (2019)
62. Dobbs, N., "STING activation by translocation from the ER is associated with infection and autoinflammatory disease", Cell Host Microbe, 18, pp.157~168 (2015)
63. Zhao, B., "A conserved PLPLRT", SD motif of STING mediates the recruitment and activation of TBK1, 2019, pp.569, 718~722
64. Zhao, B., "Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins", Proc. Natl. Acad. Sci. USA, 113, pp.E3403~E3412 (2016)
65. Uzé, G., "Genetic transfer of a functional human interferon alpha receptor into mouse cells : cloning and expression of its cDNA", Cell, 60, pp.225~234 (1990)
66. Novick, D., "The human interferon alpha", beta receptor : characterization and molecular cloning, 1994, pp.77, 391~400
67. Cohen, B., "Ligand-induced association of the type I interferon receptor components", Mol. Cell. Biol, 15, pp.4208~4214 (1995)
68. Ivashkiv, L. B., "Regulation of type I interferon responses", Nat. Rev. Immunol, 14, pp.36~49 (2014)
69. Schoggins, J. W., "A diverse range of gene products are effectors of the type I interferon antiviral response", Nature, 472, pp.481~485 (2011)
70. Hou, Y., "Non-canonical NF-κB antagonizes STING sensor-mediated DNA sensing in radiotherapy", Immunity, 49, pp.490~503 (2018)
71. Fang, R., "NEMO-IKKβ are essential for IRF3 and NF-κB activation in the cGAS-STING pathway", J. Immunol, 199, pp.3222~3233 (2017)
72. Abe, T., "Cytosolic-DNA-mediated, STING-dependent proinflammatory gene induction necessitates canonical NF-kappaB activation through TBK1", J. Virol, 88, pp.5328~5341 (2014)
73. Balka, K. R., "TBK1 and IKKε act redundantly to mediate STING-induced NF-κB responses in myeloid cells", Cell Rep, 31, pp.107492~ (2020)
74. de Oliveira Mann, C. C., "Modular architecture of the STING C-terminal tail allows interferon and NF-κB signaling adaptation", Cell Rep, 27, pp.1165~1175 (2019)
75. Cerboni, S., "Intrinsic antiproliferative activity of the innate sensor STING in T lymphocytes", J. Exp. Med, 214, pp.1769~1785 (2017)
76. Bakhoum, S. F., "Chromosomal instability drives metastasis through a cytosolic DNA response", Nature, 553, pp.467~472 (2018)
77. Tsuchida, T., "The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA", Immunity, 33, pp.765~776 (2010)
78. Yang, L., "UBXN3B positively regulates STING-mediated antiviral immune responses", Nat. Commun, 9, pp.2329~ (2018)
79. Yang, B., "RNF90 negatively regulates cellular antiviral responses by targeting MITA for degradation", PLoS Pathog, 16, pp.e1008387~ (2020)
80. Zhong, B., "The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA", Immunity, 30, pp.397~407 (2009)
81. Zhang, J., "TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA", STING protein for K63-linked ubiquitination, 2012, pp.287, 28646~28655
82. Wang, Q., "The E3 ubiquitin ligase AMFR and INSIG1 bridge the activation of TBK1 kinase by modifying the adaptor STING", Immunity, 41, pp.919~933 (2014)
83. Zhang, Z. D., "RNF115 plays dual roles in innate antiviral responses by catalyzing distinct ubiquitination of MAVS and MITA", Nat. Commun, 11, pp.5536~ (2020)
84. Qin, Y., "RNF26 temporally regulates virus-triggered type I interferon induction by two distinct mechanisms", PLoS Pathog, 10, pp.e1004358~ (2014)
85. Ni, G., "Ubiquitination of STING at lysine 224 controls IRF3 activation", Sci. Immunol, 2, pp.eaah7119~ (2017)
86. Wang, Y., "TRIM30α is a negative-feedback regulator of the intracellular DNA and DNA virus-triggered response by targeting STING", PLoS Pathog, 11, pp.e1005012~ (2015)
87. Li, Q., "TRIM29 negatively controls antiviral immune response through targeting STING for degradation", Cell Disco, 4, pp.13~ (2018)
88. Li, X., "The transmembrane endoplasmic reticulum-associated E3 ubiquitin ligase TRIM13 restrains the pathogenic-DNA-triggered inflammatory response", Sci. Adv, 8, pp.eabh0496~ (2022)
89. Kraus, F., "Function and regulation of the divisome for mitochondrial fission", Nature, 590, pp.57~66 (2021)
90. Gehrke, N., "Oxidative damage of DNA confers resistance to cytosolic nuclease TREX1 degradation and potentiates STING-dependent immune sensing", Immunity, 39, pp.482~495 (2013)
91. Stetson, D. B., "Trex1 prevents cell-intrinsic initiation of autoimmunity", Cell, 134, pp.587~598 (2008)
92. Peschke, K., "Loss of Trex1 in dendritic cells is sufficient to trigger systemic autoimmunity", J. Immunol, 197, pp.2157~2166 (2016)
93. Caielli, S., "Oxidized mitochondrial nucleoids released by neutrophils drive type I interferon production in human lupus", J. Exp. Med, 213, pp.697~713 (2016)
94. Lood, C., "Neutrophil extracellular traps enriched in oxidized mitochondrial DNA are interferogenic and contribute to lupus-like disease", Nat. Med, 22, pp.146~153 (2016)
95. Xian, H., "Oxidized DNA fragments exit mitochondria via mPTP-and VDACdependent channels to activate NLRP3 inflammasome and interferon signaling", Immunity, 55, pp.1370~1385 (2022)
96. Orzalli, M. H., "An antiviral branch of the IL-1 signaling pathway restricts immune-evasive virus replication", Mol. Cell, 71, pp.825~840 (2018)
97. Aarreberg, L. D., "Interleukin-1β Induces mtDNA release to activate innate immune signaling via cGAS-STING", Mol. Cell, 74, pp.801~815 (2019)
98. Kim, J., "VDAC oligomers form mitochondrial pores to release mtDNA fragments and promote lupus-like disease", Science, 366, pp.1531~1536 (2019)
99. Baines, C. P., "Molkentin, J. D. Voltagedependent anion channels are dispensable for mitochondrial-dependent cell death", Nat. Cell Biol, 9, pp.550~555 (2007)
100. Sprenger, H. G., "Cellular pyrimidine imbalance triggers mitochondrial DNAdependent innate immunity", Nat. Metab, 3, pp.636~650 (2021)
101. Huang, Y., "Brown adipose TRX2 deficiency activates mtDNA-NLRP3 to impair thermogenesis and protect against diet-induced insulin resistance", J. Clin. Invest, 132, pp.e148852~ (2022)
102. Rongvaux, A., "Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA", Cell, 159, pp.1563~1577 (2014)
103. Merry, D. E, "Bcl-2 gene family in the nervous system", Annu. Rev. Neurosci, 20, pp.245~267 (1997)
104. Shimizu, S., "Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC", Nature, 399, pp.483~487 (1999)
105. Schafer, Z. T., "The apoptosome : physiological, developmental, and pathological modes of regulation", Dev. Cell, 10, pp.549~561 (2006)
106. Li, S., "SFTSV infection induces BAK", BAX-dependent mitochondrial DNA release to trigger NLRP3 inflammasome activation, 2020, pp.30, 4370~4385
107. Lindqvist, L. M., "Autophagy induced during apoptosis degrades mitochondria and inhibits type I interferon secretion", Cell Death Differ, 25, pp.784~796 (2018)
108. White, M. J., "Apoptotic caspases suppress mtDNA-induced STING-mediated type I IFN production", Cell, 159, pp.1549~1562 (2014)
109. McArthur, K., "BAK", BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis, 2018, pp.359, eaao6047~
110. Riley, J. S., "Mitochondrial inner membrane permeabilisation enables mtDNA release during apoptosis", EMBO J, 37, pp.e99238~ (2018)
111. Shoshan-Barmatz, V., "VDAC1 functions in Ca(2+)homeostasis and cell life and death in health and disease", Cell Calcium, 69, pp.81~100 (2018)
112. Krause, J., "Cross-linking analysis of yeast mitochondrial outer membrane", Biochim. Biophys. Acta, 860, pp.690~698 (1986)
113. Zalk, R., "Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria", Biochem. J, 386, pp.73~83 (2005)
114. Domizio, J. D., "The cGAS-STING pathway drives type I IFN immunopathology in COVID-19", Nature, 603, pp.145~151 (2022)
115. Yu, C. H., "TDP-43 Triggers Mitochondrial DNA Release via mPTP to Activate cGAS", STING in ALS, 2020, pp.183, 636~649

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