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Volumn 74, Issue 2, 2015, Pages 198-206

LGP2 synergy with MDA5 in RLR-mediated RNA recognition and antiviral signaling

Author keywords

Antiviral immunity; LGP2; MDA5; RIG I like receptors

Indexed keywords

ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED RNA; LABORATORY OF GENETICS AND PHYSIOLOGY 2 PROTEIN; PROTEIN MDA5; RETINOIC ACID INDUCIBLE GENE I LIKE RECEPTOR; RETINOIC ACID INDUCIBLE PROTEIN I; RNA; RNA HELICASE; UNCLASSIFIED DRUG; DDX58 PROTEIN, HUMAN; DEAD BOX PROTEIN; DHX58 PROTEIN, HUMAN; IFIH1 PROTEIN, HUMAN; INTERFERON INDUCED HELICASE C DOMAIN CONTAINING PROTEIN 1; VIRUS RNA;

EID: 84949725975     PISSN: 10434666     EISSN: 10960023     Source Type: Journal    
DOI: 10.1016/j.cyto.2015.02.010     Document Type: Review
Times cited : (96)

References (93)
  • 2
    • 84903908350 scopus 로고    scopus 로고
    • Transcriptional regulation by STAT1 and STAT2 in the interferon JAK-STAT pathway
    • Au-Yeung N., Mandhana R., Horvath C.M. Transcriptional regulation by STAT1 and STAT2 in the interferon JAK-STAT pathway. Jakstat 2013, 2:e23931.
    • (2013) Jakstat , vol.2 , pp. e23931
    • Au-Yeung, N.1    Mandhana, R.2    Horvath, C.M.3
  • 3
    • 65649083024 scopus 로고    scopus 로고
    • Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2
    • Bamming D., Horvath C.M. Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J Biol Chem 2009, 284:9700-9712.
    • (2009) J Biol Chem , vol.284 , pp. 9700-9712
    • Bamming, D.1    Horvath, C.M.2
  • 4
    • 80053590435 scopus 로고    scopus 로고
    • Orchestrating the interferon antiviral response through the mitochondrial antiviral signaling (MAVS) adapter
    • Belgnaoui S.M., Paz S., Hiscott J. Orchestrating the interferon antiviral response through the mitochondrial antiviral signaling (MAVS) adapter. Curr Opin Immunol 2011, 23:564-572.
    • (2011) Curr Opin Immunol , vol.23 , pp. 564-572
    • Belgnaoui, S.M.1    Paz, S.2    Hiscott, J.3
  • 5
    • 84859427527 scopus 로고    scopus 로고
    • MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA
    • Berke I.C., Modis Y. MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA. EMBO J 2012, 31:1714-1726.
    • (2012) EMBO J , vol.31 , pp. 1714-1726
    • Berke, I.C.1    Modis, Y.2
  • 6
    • 84873702210 scopus 로고    scopus 로고
    • Structural basis of innate immune recognition of viral RNA
    • Berke I.C., Li Y., Modis Y. Structural basis of innate immune recognition of viral RNA. Cell Microbiol 2013, 15:386-394.
    • (2013) Cell Microbiol , vol.15 , pp. 386-394
    • Berke, I.C.1    Li, Y.2    Modis, Y.3
  • 7
    • 84868538362 scopus 로고    scopus 로고
    • MDA5 assembles into a polar helical filament on dsRNA
    • Berke I.C., Yu X., Modis Y., Egelman E.H. MDA5 assembles into a polar helical filament on dsRNA. Proc Natl Acad Sci USA 2012, 109:18437-18441.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 18437-18441
    • Berke, I.C.1    Yu, X.2    Modis, Y.3    Egelman, E.H.4
  • 8
    • 84857393830 scopus 로고    scopus 로고
    • Activation of RIG-I-like receptor signal transduction
    • Bruns A.M., Horvath C.M. Activation of RIG-I-like receptor signal transduction. Crit Rev Biochem Mol Biol 2012, 47:194-206.
    • (2012) Crit Rev Biochem Mol Biol , vol.47 , pp. 194-206
    • Bruns, A.M.1    Horvath, C.M.2
  • 9
    • 84908322828 scopus 로고    scopus 로고
    • Antiviral RNA recognition and assembly by RLR family innate immune sensors
    • Bruns A.M., Horvath C.M. Antiviral RNA recognition and assembly by RLR family innate immune sensors. Cytokine Growth Factor Rev 2014, 25:507-512.
    • (2014) Cytokine Growth Factor Rev , vol.25 , pp. 507-512
    • Bruns, A.M.1    Horvath, C.M.2
  • 10
    • 84926104091 scopus 로고    scopus 로고
    • The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly
    • Bruns A.M., Leser G.P., Lamb R.A., Horvath C.M. The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly. Mol Cell 2014, 55:771-781.
    • (2014) Mol Cell , vol.55 , pp. 771-781
    • Bruns, A.M.1    Leser, G.P.2    Lamb, R.A.3    Horvath, C.M.4
  • 11
    • 84872348735 scopus 로고    scopus 로고
    • ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, laboratory of genetics and physiology 2 (LGP2)
    • Bruns A.M., Pollpeter D., Hadizadeh N., Myong S., Marko J.F., Horvath C.M. ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, laboratory of genetics and physiology 2 (LGP2). J Biol Chem 2013, 288:938-946.
    • (2013) J Biol Chem , vol.288 , pp. 938-946
    • Bruns, A.M.1    Pollpeter, D.2    Hadizadeh, N.3    Myong, S.4    Marko, J.F.5    Horvath, C.M.6
  • 12
    • 84896689557 scopus 로고    scopus 로고
    • RIG-I-like receptors evolved adaptively in mammals, with parallel evolution at LGP2 and RIG-I
    • Cagliani R., Forni D., Tresoldi C., Pozzoli U., Filippi G., Rainone V., et al. RIG-I-like receptors evolved adaptively in mammals, with parallel evolution at LGP2 and RIG-I. J Mol Biol 2014, 426:1351-1365.
    • (2014) J Mol Biol , vol.426 , pp. 1351-1365
    • Cagliani, R.1    Forni, D.2    Tresoldi, C.3    Pozzoli, U.4    Filippi, G.5    Rainone, V.6
  • 13
    • 80255141860 scopus 로고    scopus 로고
    • The RIG-I ATPase domain structure reveals insights into ATP-dependent antiviral signalling
    • Civril F., Bennett M., Moldt M., Deimling T., Witte G., Schiesser S., et al. The RIG-I ATPase domain structure reveals insights into ATP-dependent antiviral signalling. EMBO Rep 2011, 12:1127-1134.
    • (2011) EMBO Rep , vol.12 , pp. 1127-1134
    • Civril, F.1    Bennett, M.2    Moldt, M.3    Deimling, T.4    Witte, G.5    Schiesser, S.6
  • 14
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O., Banroques J., Tanner N.K., Linder P. The DEAD-box protein family of RNA helicases. Gene 2006, 367:17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 15
    • 38649089789 scopus 로고    scopus 로고
    • The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of RIG-I
    • Cui S., Eisenächer K., Kirchhofer A, Brzózka K, Lammens A, Lammens K, et al. The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of RIG-I. Mol Cell 2008, 29(2):169-179.
    • (2008) Mol Cell , vol.29 , Issue.2 , pp. 169-179
    • Cui, S.1    Eisenächer, K.2    Kirchhofer, A.3    Brzózka, K.4    Lammens, A.5    Lammens, K.6
  • 16
    • 78549284909 scopus 로고    scopus 로고
    • 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members
    • Daffis S., Szretter K.J., Schriewer J., Li J., Youn S., Errett J., et al. 2'-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature 2010, 468:452-456.
    • (2010) Nature , vol.468 , pp. 452-456
    • Daffis, S.1    Szretter, K.J.2    Schriewer, J.3    Li, J.4    Youn, S.5    Errett, J.6
  • 17
    • 84898722385 scopus 로고    scopus 로고
    • Identification of an LGP2-associated MDA5 agonist in picornavirus-infected cells
    • Deddouche S., Goubau D., Rehwinkel J., Chakravarty P., Begum S., Maillard P.V., et al. Identification of an LGP2-associated MDA5 agonist in picornavirus-infected cells. Elife 2014, 3:e01535.
    • (2014) Elife , vol.3 , pp. e01535
    • Deddouche, S.1    Goubau, D.2    Rehwinkel, J.3    Chakravarty, P.4    Begum, S.5    Maillard, P.V.6
  • 18
    • 84870476784 scopus 로고    scopus 로고
    • MDA5 detects the double-stranded RNA replicative form in picornavirus-infected cells
    • Feng Q., Hato S.V., Langereis M.A., Zoll J., Virgen-Slane R., Peisley A., et al. MDA5 detects the double-stranded RNA replicative form in picornavirus-infected cells. Cell Rep 2012, 2:1187-1196.
    • (2012) Cell Rep , vol.2 , pp. 1187-1196
    • Feng, Q.1    Hato, S.V.2    Langereis, M.A.3    Zoll, J.4    Virgen-Slane, R.5    Peisley, A.6
  • 19
    • 84903904112 scopus 로고    scopus 로고
    • STAT2 and IRF9: beyond ISGF3
    • Fink K., Grandvaux N. STAT2 and IRF9: beyond ISGF3. Jakstat 2013, 2:e27521.
    • (2013) Jakstat , vol.2 , pp. e27521
    • Fink, K.1    Grandvaux, N.2
  • 20
    • 84884134473 scopus 로고    scopus 로고
    • Extensive cooperation of immune master regulators IRF3 and NFκB in RNA Pol II recruitment and pause release in human innate antiviral transcription
    • Freaney J.E., Kim R., Mandhana R., Horvath C.M. Extensive cooperation of immune master regulators IRF3 and NFκB in RNA Pol II recruitment and pause release in human innate antiviral transcription. Cell Rep 2013, 4:959-973.
    • (2013) Cell Rep , vol.4 , pp. 959-973
    • Freaney, J.E.1    Kim, R.2    Mandhana, R.3    Horvath, C.M.4
  • 22
    • 84894028950 scopus 로고    scopus 로고
    • Autoimmune disorders associated with gain of function of the intracellular sensor MDA5
    • Funabiki M., Kato H., Miyachi Y., Toki H., Motegi H., Inoue M., et al. Autoimmune disorders associated with gain of function of the intracellular sensor MDA5. Immunity 2014, 40:199-212.
    • (2014) Immunity , vol.40 , pp. 199-212
    • Funabiki, M.1    Kato, H.2    Miyachi, Y.3    Toki, H.4    Motegi, H.5    Inoue, M.6
  • 23
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • Gack M.U., Shin Y.C., Joo C.-H., Urano T., Liang C., Sun L., et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 2007, 446:916-920.
    • (2007) Nature , vol.446 , pp. 916-920
    • Gack, M.U.1    Shin, Y.C.2    Joo, C.-H.3    Urano, T.4    Liang, C.5    Sun, L.6
  • 24
    • 33744791510 scopus 로고    scopus 로고
    • Essential role of mda-5 in type I IFN responses to polyriboinosinic-polyribocytidylic acid and encephalomyocarditis picornavirus
    • Gitlin L., Barchet W., Gilfillan S., Cella M., Beutler B., Flavell R., et al. Essential role of mda-5 in type I IFN responses to polyriboinosinic-polyribocytidylic acid and encephalomyocarditis picornavirus. Proc Natl Acad Sci USA 2006, 103:8459-8464.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8459-8464
    • Gitlin, L.1    Barchet, W.2    Gilfillan, S.3    Cella, M.4    Beutler, B.5    Flavell, R.6
  • 26
    • 84908192059 scopus 로고    scopus 로고
    • Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates
    • Goubau D., Schlee M., Deddouche S., Pruijssers A.J., Zillinger T., Goldeck M., et al. Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates. Nature 2014, 514:372-375.
    • (2014) Nature , vol.514 , pp. 372-375
    • Goubau, D.1    Schlee, M.2    Deddouche, S.3    Pruijssers, A.J.4    Zillinger, T.5    Goldeck, M.6
  • 28
    • 33748475531 scopus 로고    scopus 로고
    • Type I interferon [corrected] gene induction by the interferon regulatory factor family of transcription factors
    • Honda K., Takaoka A., Taniguchi T. Type I interferon [corrected] gene induction by the interferon regulatory factor family of transcription factors. Immunity 2006, 25:349-360.
    • (2006) Immunity , vol.25 , pp. 349-360
    • Honda, K.1    Takaoka, A.2    Taniguchi, T.3
  • 30
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou F., Sun L., Zheng H., Skaug B., Jiang Q.-X., Chen Z.J. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 2011, 146:448-461.
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.-X.5    Chen, Z.J.6
  • 31
    • 79251550124 scopus 로고    scopus 로고
    • Linear ubiquitin assembly complex negatively regulates RIG-I- and TRIM25-mediated type I interferon induction
    • Inn K.S., Gack M.U., Tokunaga F., Shi M., Wong L.Y., Iwai K., et al. Linear ubiquitin assembly complex negatively regulates RIG-I- and TRIM25-mediated type I interferon induction. Mol Cell 2011, 41:354-365.
    • (2011) Mol Cell , vol.41 , pp. 354-365
    • Inn, K.S.1    Gack, M.U.2    Tokunaga, F.3    Shi, M.4    Wong, L.Y.5    Iwai, K.6
  • 32
    • 84893075305 scopus 로고    scopus 로고
    • Regulation of type I interferon responses
    • Ivashkiv L.B., Donlin L.T. Regulation of type I interferon responses. Nat Rev Immunol 2014, 14:36-49.
    • (2014) Nat Rev Immunol , vol.14 , pp. 36-49
    • Ivashkiv, L.B.1    Donlin, L.T.2
  • 33
    • 84887990870 scopus 로고    scopus 로고
    • Mechanisms of MAVS regulation at the mitochondrial membrane
    • Jacobs J.L., Coyne C.B. Mechanisms of MAVS regulation at the mitochondrial membrane. J Mol Biol 2013, 425:5009-5019.
    • (2013) J Mol Biol , vol.425 , pp. 5009-5019
    • Jacobs, J.L.1    Coyne, C.B.2
  • 34
    • 81555204380 scopus 로고    scopus 로고
    • Structural basis of RNA recognition and activation by innate immune receptor RIG-I
    • Jiang F., Ramanathan A., Miller M.T., Tang G.-Q., Gale M., Patel S.S., et al. Structural basis of RNA recognition and activation by innate immune receptor RIG-I. Nature 2011, 479:423-427.
    • (2011) Nature , vol.479 , pp. 423-427
    • Jiang, F.1    Ramanathan, A.2    Miller, M.T.3    Tang, G.-Q.4    Gale, M.5    Patel, S.S.6
  • 35
    • 84555178934 scopus 로고    scopus 로고
    • Structural insights into the activation of RIG-I, a nanosensor for viral RNAs
    • Jiang Q.-X., Chen Z.J. Structural insights into the activation of RIG-I, a nanosensor for viral RNAs. EMBO Rep 2012, 13:7-8.
    • (2012) EMBO Rep , vol.13 , pp. 7-8
    • Jiang, Q.-X.1    Chen, Z.J.2
  • 36
    • 84862994793 scopus 로고    scopus 로고
    • Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response
    • Jiang X., Kinch L.N., Brautigam C.A., Chen X., Du F., Grishin N.V., et al. Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response. Immunity 2012, 36:959-973.
    • (2012) Immunity , vol.36 , pp. 959-973
    • Jiang, X.1    Kinch, L.N.2    Brautigam, C.A.3    Chen, X.4    Du, F.5    Grishin, N.V.6
  • 37
    • 46949097299 scopus 로고    scopus 로고
    • Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5
    • Kato H., Takeuchi O., Mikamo-Satoh E., Hirai R., Kawai T., Matsushita K., et al. Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5. J Exp Med 2008, 205:1601-1610.
    • (2008) J Exp Med , vol.205 , pp. 1601-1610
    • Kato, H.1    Takeuchi, O.2    Mikamo-Satoh, E.3    Hirai, R.4    Kawai, T.5    Matsushita, K.6
  • 38
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato H., Takeuchi O., Sato S., Yoneyama M., Yamamoto M., Matsui K., et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 2006, 441:101-105.
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1    Takeuchi, O.2    Sato, S.3    Yoneyama, M.4    Yamamoto, M.5    Matsui, K.6
  • 39
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
    • Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., et al. IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat Immunol 2005, 6:981-988.
    • (2005) Nat Immunol , vol.6 , pp. 981-988
    • Kawai, T.1    Takahashi, K.2    Sato, S.3    Coban, C.4    Kumar, H.5    Kato, H.6
  • 40
    • 33845431988 scopus 로고    scopus 로고
    • RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2
    • Komuro A., Horvath C.M. RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2. J Virol 2006, 80:12332-12342.
    • (2006) J Virol , vol.80 , pp. 12332-12342
    • Komuro, A.1    Horvath, C.M.2
  • 41
    • 51349108659 scopus 로고    scopus 로고
    • Negative regulation of cytoplasmic RNA-mediated antiviral signaling
    • Komuro A., Bamming D., Horvath C.M. Negative regulation of cytoplasmic RNA-mediated antiviral signaling. Cytokine 2008, 43:350-358.
    • (2008) Cytokine , vol.43 , pp. 350-358
    • Komuro, A.1    Bamming, D.2    Horvath, C.M.3
  • 42
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • Kowalinski E., Lunardi T., McCarthy A.A., Louber J., Brunel J., Grigorov B., et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 2011, 147:423-435.
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1    Lunardi, T.2    McCarthy, A.A.3    Louber, J.4    Brunel, J.5    Grigorov, B.6
  • 43
    • 33745814424 scopus 로고    scopus 로고
    • Essential role of IPS-1 in innate immune responses against RNA viruses
    • Kumar H., Kawai T., Kato H., Sato S., Takahashi K., Coban C., et al. Essential role of IPS-1 in innate immune responses against RNA viruses. J Exp Med 2006, 203:1795-1803.
    • (2006) J Exp Med , vol.203 , pp. 1795-1803
    • Kumar, H.1    Kawai, T.2    Kato, H.3    Sato, S.4    Takahashi, K.5    Coban, C.6
  • 44
    • 67651232539 scopus 로고    scopus 로고
    • Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5
    • Li X., Lu C., Stewart M., Xu H., Strong R.K., Igumenova T., et al. Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5. Arch Biochem Biophys 2009, 488:23-33.
    • (2009) Arch Biochem Biophys , vol.488 , pp. 23-33
    • Li, X.1    Lu, C.2    Stewart, M.3    Xu, H.4    Strong, R.K.5    Igumenova, T.6
  • 45
    • 79960724199 scopus 로고    scopus 로고
    • From unwinding to clamping - the DEAD box RNA helicase family
    • Linder P., Jankowsky E. From unwinding to clamping - the DEAD box RNA helicase family. Nat Rev Mol Cell Biol 2011, 12:505-516.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 505-516
    • Linder, P.1    Jankowsky, E.2
  • 46
    • 84882705934 scopus 로고    scopus 로고
    • MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades
    • e00785-e00785
    • Liu S., Chen J., Cai X., Wu J., Chen X., Wu Y.-T., et al. MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades. Elife 2013, 2. e00785-e00785.
    • (2013) Elife , vol.2
    • Liu, S.1    Chen, J.2    Cai, X.3    Wu, J.4    Chen, X.5    Wu, Y.-T.6
  • 48
    • 84899534322 scopus 로고    scopus 로고
    • MDA5 and autoimmune disease
    • Miner J.J., Diamond M.S. MDA5 and autoimmune disease. Nat Genet 2014, 46:418-419.
    • (2014) Nat Genet , vol.46 , pp. 418-419
    • Miner, J.J.1    Diamond, M.S.2
  • 50
    • 84873523444 scopus 로고    scopus 로고
    • Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling
    • Motz C., Schuhmann K.M., Kirchhofer A., Moldt M., Witte G., Conzelmann K.-K., et al. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science 2013, 339:690-693.
    • (2013) Science , vol.339 , pp. 690-693
    • Motz, C.1    Schuhmann, K.M.2    Kirchhofer, A.3    Moldt, M.4    Witte, G.5    Conzelmann, K.-K.6
  • 51
    • 60749124538 scopus 로고    scopus 로고
    • Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA
    • Myong S., Cui S., Cornish P.V., Kirchhofer A., Gack M.U., Jung J.U., et al. Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA. Science 2009, 323:1070-1074.
    • (2009) Science , vol.323 , pp. 1070-1074
    • Myong, S.1    Cui, S.2    Cornish, P.V.3    Kirchhofer, A.4    Gack, M.U.5    Jung, J.U.6
  • 52
    • 78650189572 scopus 로고    scopus 로고
    • The ubiquitin ligase riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection
    • Oshiumi H., Miyashita M., Inoue N., Okabe M., Matsumoto M., Seya T. The ubiquitin ligase riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection. Cell Host Microbe 2010, 8:496-509.
    • (2010) Cell Host Microbe , vol.8 , pp. 496-509
    • Oshiumi, H.1    Miyashita, M.2    Inoue, N.3    Okabe, M.4    Matsumoto, M.5    Seya, T.6
  • 53
    • 67650439286 scopus 로고    scopus 로고
    • A shared interface mediates paramyxovirus interference with antiviral RNA helicases MDA5 and LGP2
    • Parisien J.-P., Bamming D., Komuro A., Ramachandran A., Rodriguez J.J., Barber G., et al. A shared interface mediates paramyxovirus interference with antiviral RNA helicases MDA5 and LGP2. J Virol 2009, 83:7252-7260.
    • (2009) J Virol , vol.83 , pp. 7252-7260
    • Parisien, J.-P.1    Bamming, D.2    Komuro, A.3    Ramachandran, A.4    Rodriguez, J.J.5    Barber, G.6
  • 54
    • 84898718337 scopus 로고    scopus 로고
    • Three-stranded antiviral attack
    • e02369-e02369
    • Patel J.R., García-Sastre A. Three-stranded antiviral attack. Elife 2014, 3. e02369-e02369.
    • (2014) Elife , vol.3
    • Patel, J.R.1    García-Sastre, A.2
  • 55
    • 84883487585 scopus 로고    scopus 로고
    • ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon
    • Patel J.R., Jain A., Chou Y.-Y., Baum A., Ha T., García-Sastre A. ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon. EMBO Rep 2013, 14:780-787.
    • (2013) EMBO Rep , vol.14 , pp. 780-787
    • Patel, J.R.1    Jain, A.2    Chou, Y.-Y.3    Baum, A.4    Ha, T.5    García-Sastre, A.6
  • 56
    • 79960049196 scopus 로고    scopus 로고
    • A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response
    • Paz S., Vilasco M., Werden S.J., Arguello M., Joseph-Pillai D., Zhao T., et al. A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response. Cell Res 2011, 21:895-910.
    • (2011) Cell Res , vol.21 , pp. 895-910
    • Paz, S.1    Vilasco, M.2    Werden, S.J.3    Arguello, M.4    Joseph-Pillai, D.5    Zhao, T.6
  • 57
    • 84870614532 scopus 로고    scopus 로고
    • Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments
    • Peisley A., Jo M.H., Lin C., Wu B., Orme-Johnson M., Walz T., et al. Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments. Proc Natl Acad Sci USA 2012, 109:E3340-E3349.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. E3340-E3349
    • Peisley, A.1    Jo, M.H.2    Lin, C.3    Wu, B.4    Orme-Johnson, M.5    Walz, T.6
  • 58
    • 84862909216 scopus 로고    scopus 로고
    • Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition
    • Peisley A., Lin C., Wu B., Orme-Johnson M., Liu M., Walz T., et al. Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition. Proc Natl Acad Sci USA 2011, 108:21010-21015.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 21010-21015
    • Peisley, A.1    Lin, C.2    Wu, B.3    Orme-Johnson, M.4    Liu, M.5    Walz, T.6
  • 59
    • 84899957213 scopus 로고    scopus 로고
    • Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I
    • Peisley A., Wu B., Xu H., Chen Z.J., Hur S. Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature 2014, 509.
    • (2014) Nature , pp. 509
    • Peisley, A.1    Wu, B.2    Xu, H.3    Chen, Z.J.4    Hur, S.5
  • 60
    • 84883759334 scopus 로고    scopus 로고
    • RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner
    • Peisley A., Wu B., Yao H., Walz T., Hur S. RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner. Mol Cell 2013, 51:573-583.
    • (2013) Mol Cell , vol.51 , pp. 573-583
    • Peisley, A.1    Wu, B.2    Yao, H.3    Walz, T.4    Hur, S.5
  • 61
    • 70349728538 scopus 로고    scopus 로고
    • Activation of MDA5 requires higher-order RNA structures generated during virus infection
    • Pichlmair A., Schulz O., Tan C.-P., Rehwinkel J., Kato H., Takeuchi O., et al. Activation of MDA5 requires higher-order RNA structures generated during virus infection. J Virol 2009, 83:10761-10769.
    • (2009) J Virol , vol.83 , pp. 10761-10769
    • Pichlmair, A.1    Schulz, O.2    Tan, C.-P.3    Rehwinkel, J.4    Kato, H.5    Takeuchi, O.6
  • 63
    • 79954989343 scopus 로고    scopus 로고
    • Impaired cellular responses to cytosolic DNA or infection with Listeria monocytogenes and vaccinia virus in the absence of the murine LGP2 protein
    • Pollpeter D., Komuro A., Barber G.N., Horvath C.M. Impaired cellular responses to cytosolic DNA or infection with Listeria monocytogenes and vaccinia virus in the absence of the murine LGP2 protein. PLoS ONE 2011, 6:e18842.
    • (2011) PLoS ONE , vol.6 , pp. e18842
    • Pollpeter, D.1    Komuro, A.2    Barber, G.N.3    Horvath, C.M.4
  • 64
    • 79959649316 scopus 로고    scopus 로고
    • RIG-I like receptors and their signaling crosstalk in the regulation of antiviral immunity
    • Ramos H.J., Gale M. RIG-I like receptors and their signaling crosstalk in the regulation of antiviral immunity. Curr Opin Virol 2011, 1:167-176.
    • (2011) Curr Opin Virol , vol.1 , pp. 167-176
    • Ramos, H.J.1    Gale, M.2
  • 65
    • 84890851204 scopus 로고    scopus 로고
    • Parts, assembly and operation of the RIG-I family of motors
    • Rawling D.C., Pyle A.M. Parts, assembly and operation of the RIG-I family of motors. Curr Opin Struct Biol 2014, 25C:25-33.
    • (2014) Curr Opin Struct Biol , vol.25C , pp. 25-33
    • Rawling, D.C.1    Pyle, A.M.2
  • 66
    • 84899495767 scopus 로고    scopus 로고
    • Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling
    • Rice G.I., del Toro Duany Y., Jenkinson E.M., Forte G.M.A., Anderson B.H., Ariaudo G., et al. Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling. Nat Genet 2014, 46:503-509.
    • (2014) Nat Genet , vol.46 , pp. 503-509
    • Rice, G.I.1    del Toro Duany, Y.2    Jenkinson, E.M.3    Forte, G.M.A.4    Anderson, B.H.5    Ariaudo, G.6
  • 67
    • 80051619284 scopus 로고    scopus 로고
    • Autoimmune disease risk variant of IFIH1 is associated with increased sensitivity to IFN-α and serologic autoimmunity in lupus patients
    • Robinson T., Kariuki S.N., Franek B.S., Kumabe M., Kumar A.A., Badaracco M., et al. Autoimmune disease risk variant of IFIH1 is associated with increased sensitivity to IFN-α and serologic autoimmunity in lupus patients. J Immunol 2011, 187:1298-1303.
    • (2011) J Immunol , vol.187 , pp. 1298-1303
    • Robinson, T.1    Kariuki, S.N.2    Franek, B.S.3    Kumabe, M.4    Kumar, A.A.5    Badaracco, M.6
  • 68
    • 84874675342 scopus 로고    scopus 로고
    • Amino acid requirements for MDA5 and LGP2 recognition by paramyxovirus V proteins: a single arginine distinguishes MDA5 from RIG-I
    • Rodriguez K.R., Horvath C.M. Amino acid requirements for MDA5 and LGP2 recognition by paramyxovirus V proteins: a single arginine distinguishes MDA5 from RIG-I. J Virol 2013, 87:2974-2978.
    • (2013) J Virol , vol.87 , pp. 2974-2978
    • Rodriguez, K.R.1    Horvath, C.M.2
  • 69
    • 84903880722 scopus 로고    scopus 로고
    • MDA5 and LGP2: accomplices and antagonists of antiviral signal transduction
    • 00640-14
    • Rodriguez K.R., Bruns A.M., Horvath C.M. MDA5 and LGP2: accomplices and antagonists of antiviral signal transduction. J Virol JVI. 2014, 00640-14.
    • (2014) J Virol JVI.
    • Rodriguez, K.R.1    Bruns, A.M.2    Horvath, C.M.3
  • 70
    • 26844503987 scopus 로고    scopus 로고
    • The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I
    • Rothenfusser S., Goutagny N., DiPerna G., Gong M., Monks B.G., Schoenemeyer A., et al. The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I. J Immunol 2005, 175:5260-5268.
    • (2005) J Immunol , vol.175 , pp. 5260-5268
    • Rothenfusser, S.1    Goutagny, N.2    DiPerna, G.3    Gong, M.4    Monks, B.G.5    Schoenemeyer, A.6
  • 71
    • 33846307026 scopus 로고    scopus 로고
    • Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2
    • Saito T., Hirai R., Loo Y.-M., Owen D., Johnson C.L., Sinha S.C., et al. Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. Proc Natl Acad Sci USA 2007, 104:582-587.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 582-587
    • Saito, T.1    Hirai, R.2    Loo, Y.-M.3    Owen, D.4    Johnson, C.L.5    Sinha, S.C.6
  • 72
    • 47949092573 scopus 로고    scopus 로고
    • Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA
    • Saito T, Owen D.M., Jiang F, Marcotrigiano J, Gale M. Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA. Nature 2008, 454:523-527.
    • (2008) Nature , vol.454 , pp. 523-527
    • Saito, T.1    Owen, D.M.2    Jiang, F.3    Marcotrigiano, J.4    Gale, M.5
  • 74
    • 84884157315 scopus 로고    scopus 로고
    • Master sensors of pathogenic RNA - RIG-I like receptors
    • Schlee M. Master sensors of pathogenic RNA - RIG-I like receptors. Immunobiology 2013, 218:1322-1335.
    • (2013) Immunobiology , vol.218 , pp. 1322-1335
    • Schlee, M.1
  • 75
    • 77954242369 scopus 로고    scopus 로고
    • The chase for the RIG-I ligand-recent advances
    • Schlee M., Hartmann G. The chase for the RIG-I ligand-recent advances. Mol Ther 2010, 1-9.
    • (2010) Mol Ther , pp. 1-9
    • Schlee, M.1    Hartmann, G.2
  • 76
    • 68049089651 scopus 로고    scopus 로고
    • Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus
    • Schlee M., Roth A., Hornung V., Hagmann C.A., Wimmenauer V., Barchet W., et al. Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity 2009, 31:25-34.
    • (2009) Immunity , vol.31 , pp. 25-34
    • Schlee, M.1    Roth, A.2    Hornung, V.3    Hagmann, C.A.4    Wimmenauer, V.5    Barchet, W.6
  • 77
    • 67749133995 scopus 로고    scopus 로고
    • 5'-triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I
    • Schmidt A., Schwerd T., Hamm W., Hellmuth J.C., Cui S., Wenzel M., et al. 5'-triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I. Proc Natl Acad Sci USA 2009, 106:12067-12072.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12067-12072
    • Schmidt, A.1    Schwerd, T.2    Hamm, W.3    Hellmuth, J.C.4    Cui, S.5    Wenzel, M.6
  • 78
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • Seth R.B., Sun L., Ea C.-K., Chen Z.J. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 2005, 122:669-682.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.-K.3    Chen, Z.J.4
  • 79
    • 33745240931 scopus 로고    scopus 로고
    • A genome-wide association study of nonsynonymous SNPs identifies a type 1 diabetes locus in the interferon-induced helicase (IFIH1) region
    • Smyth D.J., Cooper J.D., Bailey R., Field S., Burren O., Smink L.J., et al. A genome-wide association study of nonsynonymous SNPs identifies a type 1 diabetes locus in the interferon-induced helicase (IFIH1) region. Nat Genet 2006, 38:617-619.
    • (2006) Nat Genet , vol.38 , pp. 617-619
    • Smyth, D.J.1    Cooper, J.D.2    Bailey, R.3    Field, S.4    Burren, O.5    Smink, L.J.6
  • 80
    • 33646592188 scopus 로고    scopus 로고
    • The specific and essential role of MAVS in antiviral innate immune responses
    • Sun Q., Sun L., Liu H.-H., Chen X., Seth R.B., Forman J., et al. The specific and essential role of MAVS in antiviral innate immune responses. Immunity 2006, 24:633-642.
    • (2006) Immunity , vol.24 , pp. 633-642
    • Sun, Q.1    Sun, L.2    Liu, H.-H.3    Chen, X.4    Seth, R.B.5    Forman, J.6
  • 82
    • 39649092731 scopus 로고    scopus 로고
    • Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses
    • Takahasi K., Yoneyama M., Nishihori T., Hirai R., Kumeta H., Narita R., et al. Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses. Mol Cell 2008, 29(4):428-440.
    • (2008) Mol Cell , vol.29 , Issue.4 , pp. 428-440
    • Takahasi, K.1    Yoneyama, M.2    Nishihori, T.3    Hirai, R.4    Kumeta, H.5    Narita, R.6
  • 83
    • 67650510680 scopus 로고    scopus 로고
    • Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors
    • Takahasi K., Kumeta H., Tsuduki N., Narita R., Shigemoto T., Hirai R., et al. Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors. J Biol Chem 2009, 284:17465-17474.
    • (2009) J Biol Chem , vol.284 , pp. 17465-17474
    • Takahasi, K.1    Kumeta, H.2    Tsuduki, N.3    Narita, R.4    Shigemoto, T.5    Hirai, R.6
  • 84
    • 34248168157 scopus 로고    scopus 로고
    • Loss of DExD/H box RNA helicase LGP2 manifests disparate antiviral responses
    • Venkataraman T., Valdes M., Elsby R., Kakuta S., Caceres G., Saijo S., et al. Loss of DExD/H box RNA helicase LGP2 manifests disparate antiviral responses. J Immunol 2007, 178:6444-6455.
    • (2007) J Immunol , vol.178 , pp. 6444-6455
    • Venkataraman, T.1    Valdes, M.2    Elsby, R.3    Kakuta, S.4    Caceres, G.5    Saijo, S.6
  • 86
    • 84875542059 scopus 로고    scopus 로고
    • Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling
    • Wies E., Wang M.K., Maharaj N.P., Chen K., Zhou S., Finberg R.W., et al. Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling. Immunity 2013, 38:437-449.
    • (2013) Immunity , vol.38 , pp. 437-449
    • Wies, E.1    Wang, M.K.2    Maharaj, N.P.3    Chen, K.4    Zhou, S.5    Finberg, R.W.6
  • 87
    • 84872604349 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5
    • Wu B., Peisley A., Richards C., Yao H., Zeng X., Lin C., et al. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell 2013, 152:276-289.
    • (2013) Cell , vol.152 , pp. 276-289
    • Wu, B.1    Peisley, A.2    Richards, C.3    Yao, H.4    Zeng, X.5    Lin, C.6
  • 88
    • 84898747432 scopus 로고    scopus 로고
    • Structural basis for the prion-like MAVS filaments in antiviral innate immunity
    • Xu H., He X., Zheng H., Huang L.J., Hou F., Yu Z., et al. Structural basis for the prion-like MAVS filaments in antiviral innate immunity. Elife 2014, 3:e01489.
    • (2014) Elife , vol.3 , pp. e01489
    • Xu, H.1    He, X.2    Zheng, H.3    Huang, L.J.4    Hou, F.5    Yu, Z.6
  • 89
    • 23844438864 scopus 로고    scopus 로고
    • Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity
    • Yoneyama M., Kikuchi M., Matsumoto K., Imaizumi T., Miyagishi M., Taira K., et al. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J Immunol 2005, 175:2851-2858.
    • (2005) J Immunol , vol.175 , pp. 2851-2858
    • Yoneyama, M.1    Kikuchi, M.2    Matsumoto, K.3    Imaizumi, T.4    Miyagishi, M.5    Taira, K.6
  • 90
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama M., Kikuchi M., Natsukawa T., Shinobu N., Imaizumi T., Miyagishi M., et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol 2004, 5:730-737.
    • (2004) Nat Immunol , vol.5 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3    Shinobu, N.4    Imaizumi, T.5    Miyagishi, M.6
  • 91
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng W., Sun L., Jiang X., Chen X., Hou F., Adhikari A., et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 2010, 141:315-330.
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.1    Sun, L.2    Jiang, X.3    Chen, X.4    Hou, F.5    Adhikari, A.6
  • 92
    • 49649123561 scopus 로고    scopus 로고
    • Regulation of IkappaB kinase-related kinases and antiviral responses by tumor suppressor CYLD
    • Zhang M., Wu X., Lee A.J., Jin W., Chang M., Wright A., et al. Regulation of IkappaB kinase-related kinases and antiviral responses by tumor suppressor CYLD. J Biol Chem 2008, 283:18621-18626.
    • (2008) J Biol Chem , vol.283 , pp. 18621-18626
    • Zhang, M.1    Wu, X.2    Lee, A.J.3    Jin, W.4    Chang, M.5    Wright, A.6
  • 93
    • 78751637122 scopus 로고    scopus 로고
    • Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
    • Zust R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., et al. Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat Immunol 2011, 12:137-143.
    • (2011) Nat Immunol , vol.12 , pp. 137-143
    • Zust, R.1    Cervantes-Barragan, L.2    Habjan, M.3    Maier, R.4    Neuman, B.W.5    Ziebuhr, J.6


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