Sensors of Intracellular Nucleic Acids Activating STING-Dependent Production of Interferons in Immunocompetent Cells

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Currently, foreign DNA or RNA sensor proteins, which play an important role in innate immunity, are of great interest as a new avenue for cancer immunotherapy. Agonists of these proteins can activate signaling cascades in immune cells that cause the production of cytokines, in particular type I interferons, which have a powerful cytotoxic effect. This review examines the functioning of cytoplasmic nucleic acid sensors such as cGAS, STING, IFI16, AIM2, DAI, DDX41, DNA-PK, MRE-11, and TREX1 involved in activating the production of various cytokines.

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L. Smolyaninova

Research Institute of Experimental Diagnostics and Therapy of Tumors, N. N. Blokhin National Medical Research Center of Oncology

Email: smolyaninovalarisa1@gmail.com
俄罗斯联邦, Moscow, 115478

O. Solopova

Research Institute of Experimental Diagnostics and Therapy of Tumors, N. N. Blokhin National Medical Research Center of Oncology

编辑信件的主要联系方式.
Email: smolyaninovalarisa1@gmail.com
俄罗斯联邦, Moscow, 115478

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2. Fig. 1. Cytoplasmic nucleic acid sensors involved in activation of the STING signaling pathway and inducing type I interferon production.

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3. Fig. 2. Schematic of the domain organization of human cGAS (a) and a model of the cGAS-DNA (2:2) complex (b), in which each cGAS monomer interacts with DNA (adapted from [10, 11], used with permission of the publisher).

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4. Fig. 3. Schematic of the domain organization of the human STING protein (a) and the model of the ligand-STING complex (b) (adapted from [27], used with permission of the publisher).

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5. Fig. 4. Schematic of the domain organization of the mouse IFI16 protein (a) and a model of the dcDNA complex with HINa- and HINb-domains linked by a linker (red) (b) (adapted from [51], used with permission of the publisher).

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6. Fig. 5. Schematic of the domain organization of AIM2 (a) and model of the structure of the PYD domain (lemon color) and the dcDNA-AIM2 complex (b) (adapted from [63], used with permission of the publisher). OB1, OB2 - oligonucleotide/oligosaccharide binding folds within the HIN200 domain.

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7. Fig. 6. Schematic of the domain organization of ZBP1 (a) and model of the structure of the Z-DNA complex with two ZBP1 molecules (b) (adapted from [71, 74], used with permission of the publisher). a - Zα- and Zβ-domains binding the Z-form of DNA are shown in pink; the D3-region involved in the binding of the right-twisted B-form of DNA is shown in yellow. b - dcDNA (brown), ZBP1 molecules (purple).

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8. Fig. 7. Schematic of the domain organization of DDX41 (a), structure model of the closed conformation of the DEAD domain (b), and docking model of the DEAD domain complex bound to dcDNA (c) (adapted from [85, 86], used with permission of the publisher).

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9. Fig. 8. Schematic of the domain organization of DNA-PKcs (a) and human Ku70, Ku80 subunits (b), model of the secondary structure of the dimeric complex of Ku80 (purple) and Ku70 (red) subunits (c) and the DNA complex (yellow-orange) with the Ku70-Ku80 heterodimer (d) (adapted from [94-96], used with permission of the publisher). The amino acid after which the Ku70 subunit-specific amino acid sequence begins is marked with a blue filled dot.

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10. Fig. 9. Schematic of the domain organization of MRE-11 (a) and a model of the E. coli MRE11-RAD50 complex in the resting state (b) and in the DNA-bound state (c) (adapted from [102, 103], used with permission of the publisher). DNA binding causes a shift in nucleotide-binding domains (NBDs) and rearrangements in MRE-11, leading to channel formation in the active center region and clamping of DNA ends. HLH - helix-loop-helix, CC - double helix.

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11. Fig. 10. Schematic of TREX1 domain organization (a) and model of the TREX1 homodimer structure (b) (adapted from [106, 107], used with permission of the publisher). b - TREX1 monomers are indicated in blue and purple. The black square indicates the active center region where magnesium ions (green spheres) and dTMP nucleotide (yellow-orange structure) bind and ocDNA binding occurs. A disordered loop (166-174 a. o.) is present within the monomer and is involved in binding to dcDNA. The position of the loop is labeled Ala165 and Lys175.

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