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Volumn 109, Issue 45, 2012, Pages 18437-18441

MDA5 assembles into a polar helical filament on dsRNA

Author keywords

DExD H box RNA helicase; Innate immune receptor; Ligand binding cooperativity; Nucleic acid sensor; Prion like switch

Indexed keywords

DOUBLE STRANDED RNA; MELANOMA DIFFERENTIATION ASSOCIATED PROTEIN 5; MITOCHONDRIAL ANTIVIRAL SIGNALING PROTEIN; ONCOPROTEIN; PEPTIDES AND PROTEINS; UNCLASSIFIED DRUG;

EID: 84868538362     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212186109     Document Type: Article
Times cited : (99)

References (31)
  • 1
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato H, et al. (2006) Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441(7089):101-105.
    • (2006) Nature , vol.441 , Issue.7089 , pp. 101-105
    • Kato, H.1
  • 2
    • 33750976374 scopus 로고    scopus 로고
    • 5′-Triphosphate RNA is the ligand for RIG-I
    • Hornung V, et al. (2006) 5′-Triphosphate RNA is the ligand for RIG-I. Science 314 (5801):994-997.
    • (2006) Science , vol.314 , Issue.5801 , pp. 994-997
    • Hornung, V.1
  • 3
    • 33750984771 scopus 로고    scopus 로고
    • RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates
    • Pichlmair A, et al. (2006) RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates. Science 314(5801):997-1001.
    • (2006) Science , vol.314 , Issue.5801 , pp. 997-1001
    • Pichlmair, A.1
  • 4
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern- Recognition receptor RIG-I by viral RNA
    • Kowalinski E, et al. (2011) Structural basis for the activation of innate immune pattern- recognition receptor RIG-I by viral RNA. Cell 147(2):423-435.
    • (2011) Cell , vol.147 , Issue.2 , pp. 423-435
    • Kowalinski, E.1
  • 5
    • 81555204380 scopus 로고    scopus 로고
    • Structural basis of RNA recognition and activation by innate immune receptor RIG-I
    • Jiang F, et al. (2011) Structural basis of RNA recognition and activation by innate immune receptor RIG-I. Nature 479(7373):423-427.
    • (2011) Nature , vol.479 , Issue.7373 , pp. 423-427
    • Jiang, F.1
  • 6
    • 80054685883 scopus 로고    scopus 로고
    • Structural insights into RNA recognition by RIG-I
    • Luo D, et al. (2011) Structural insights into RNA recognition by RIG-I. Cell 147(2): 409-422.
    • (2011) Cell , vol.147 , Issue.2 , pp. 409-422
    • Luo, D.1
  • 7
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng W, et al. (2010) Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 141(2):315-330.
    • (2010) Cell , vol.141 , Issue.2 , pp. 315-330
    • Zeng, W.1
  • 8
    • 84859427527 scopus 로고    scopus 로고
    • MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA
    • Berke IC, Modis Y (2012) MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA. EMBO J 31(7):1714-1726.
    • (2012) EMBO J , vol.31 , Issue.7 , pp. 1714-1726
    • Berke, I.C.1    Modis, Y.2
  • 9
    • 84862909216 scopus 로고    scopus 로고
    • Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition
    • Peisley A, et al. (2011) Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition. Proc Natl Acad Sci USA 108(52):21010-21015.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.52 , pp. 21010-21015
    • Peisley, A.1
  • 10
    • 67651232539 scopus 로고    scopus 로고
    • Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5
    • Li X, et al. (2009) Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5. Arch Biochem Biophys 488(1):23-33.
    • (2009) Arch Biochem Biophys , vol.488 , Issue.1 , pp. 23-33
    • Li, X.1
  • 11
    • 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, et al. (2009) 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 284(26):17465-17474.
    • (2009) J Biol Chem , vol.284 , Issue.26 , pp. 17465-17474
    • Takahasi, K.1
  • 12
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou F, et al. (2011) MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146(3):448-461.
    • (2011) Cell , vol.146 , Issue.3 , pp. 448-461
    • Hou, F.1
  • 13
    • 84862994793 scopus 로고    scopus 로고
    • Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response
    • Jiang X, et al. (2012) Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response. Immunity 36(6):959-973.
    • (2012) Immunity , vol.36 , Issue.6 , pp. 959-973
    • Jiang, X.1
  • 14
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman EH (2000) A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85(4):225-234.
    • (2000) Ultramicroscopy , vol.85 , Issue.4 , pp. 225-234
    • Egelman, E.H.1
  • 15
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman EH, Francis N, DeRosier DJ (1982) F-actin is a helix with a random variable twist. Nature 298(5870):131-135.
    • (1982) Nature , vol.298 , Issue.5870 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 16
    • 0019343461 scopus 로고
    • Preparing biological samples for stereomicroscopy by the quick-freeze, deep-etch, rotary-replication technique
    • Heuser J (1981) Preparing biological samples for stereomicroscopy by the quick-freeze, deep-etch, rotary-replication technique. Methods Cell Biol 22:97-122.
    • (1981) Methods Cell Biol , vol.22 , pp. 97-122
    • Heuser, J.1
  • 17
    • 80051952088 scopus 로고    scopus 로고
    • Innate immune responses in human monocyte-derived dendritic cells are highly dependent on the size and the 5? phosphorylation of RNA molecules
    • Jiang M, et al. (2011) Innate immune responses in human monocyte-derived dendritic cells are highly dependent on the size and the 5? phosphorylation of RNA molecules. J Immunol 187(4):1713-1721.
    • (2011) J Immunol , vol.187 , Issue.4 , pp. 1713-1721
    • Jiang, M.1
  • 18
    • 65649083024 scopus 로고    scopus 로고
    • Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2
    • Bamming D, Horvath CM(2009) Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J Biol Chem284(15):9700-9712.
    • (2009) J Biol Chem , vol.284 , Issue.15 , pp. 9700-9712
    • Bamming, D.1    Horvath, C.M.2
  • 19
    • 77957750708 scopus 로고    scopus 로고
    • Loss-of-function mutations E6 27X and I923V of IFIH1 are associated with lower poly(I:C)-induced interferon- β production in peripheral blood mononuclear cells of type 1 diabetes patients
    • Chistiakov DA, Voronova NV, Savost'Anov KV, Turakulov RI (2010) Loss-of-function mutations E6 27X and I923V of IFIH1 are associated with lower poly(I:C)-induced interferon- β production in peripheral blood mononuclear cells of type 1 diabetes patients. Hum Immunol 71(11):1128-1134.
    • (2010) Hum Immunol , vol.71 , Issue.11 , pp. 1128-1134
    • Chistiakov, D.A.1    Voronova, N.V.2    Savost'Anov, K.V.3    Turakulov, R.I.4
  • 20
    • 67649415364 scopus 로고    scopus 로고
    • Identification of loss of function mutations in human genes encoding RIG-I and MDA5: Implications for resistance to type I diabetes
    • Shigemoto T, et al. (2009) Identification of loss of function mutations in human genes encoding RIG-I and MDA5: Implications for resistance to type I diabetes. J Biol Chem 284(20):13348-13354.
    • (2009) J Biol Chem , vol.284 , Issue.20 , pp. 13348-13354
    • Shigemoto, T.1
  • 21
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • Park HH, et al. (2007) Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell 128(3):533-546.
    • (2007) Cell , vol.128 , Issue.3 , pp. 533-546
    • Park, H.H.1
  • 22
    • 77953714711 scopus 로고    scopus 로고
    • Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling
    • Lin SC, Lo YC, Wu H (2010) Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 465(7300):885-890.
    • (2010) Nature , vol.465 , Issue.7300 , pp. 885-890
    • Lin, S.C.1    Lo, Y.C.2    Wu, H.3
  • 23
    • 78649635776 scopus 로고    scopus 로고
    • Molecular cell death platforms and assemblies
    • Mace PD, Riedl SJ (2010) Molecular cell death platforms and assemblies. Curr Opin Cell Biol 22(6):828-836.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.6 , pp. 828-836
    • Mace, P.D.1    Riedl, S.J.2
  • 24
    • 0036209661 scopus 로고    scopus 로고
    • Activation of the interferon-beta promoter during hepatitis C virus RNA replication
    • Fredericksen B, et al. (2002) Activation of the interferon-beta promoter during hepatitis C virus RNA replication. Viral Immunol 15(1):29-40.
    • (2002) Viral Immunol , vol.15 , Issue.1 , pp. 29-40
    • Fredericksen, B.1
  • 25
    • 26844503987 scopus 로고    scopus 로고
    • The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I
    • Rothenfusser S, et al. (2005) The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I. J Immunol 175(8):5260-5268.
    • (2005) J Immunol , vol.175 , Issue.8 , pp. 5260-5268
    • Rothenfusser, S.1
  • 26
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128(1):82-97.
    • (1999) J Struct Biol , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 27
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, et al. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116(1):190-199.
    • (1996) J Struct Biol , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1
  • 28
    • 38049034590 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Eswar N, et al. (2006) Comparative protein structure modeling using Modeller. Curr Protoc Bioinformatics 15:5.6.1-5.6.30.
    • (2006) Curr Protoc Bioinformatics , vol.15
    • Eswar, N.1
  • 29
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera - a visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1
  • 30
    • 77955358961 scopus 로고    scopus 로고
    • Using Situs for the integration of multi-resolution structures
    • Wriggers W (2010) Using Situs for the integration of multi-resolution structures. Biophys Rev 2(1):21-27.
    • (2010) Biophys Rev , vol.2 , Issue.1 , pp. 21-27
    • Wriggers, W.1
  • 31
    • 78649763344 scopus 로고    scopus 로고
    • Automated minimization of steric clashes in protein structures
    • Ramachandran S, Kota P, Ding F, Dokholyan NV (2011) Automated minimization of steric clashes in protein structures. Proteins 79(1):261-270.
    • (2011) Proteins , vol.79 , Issue.1 , pp. 261-270
    • Ramachandran, S.1    Kota, P.2    Ding, F.3    Dokholyan, N.V.4


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