Prion-like behavior of MAVS in RIG-I signaling

Cell Research

Volumn 21, Issue 12, 2011, Pages 1643-1645

  Moresco, Eva Marie Y ^a   Vine, Diantha La ^a   Beutler, Bruce ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DDX58 PROTEIN, HUMAN; DEAD BOX PROTEIN; RECOMBINANT PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; UBIQUITIN; VISA PROTEIN, HUMAN;

ARTICLE; CHEMICAL STRUCTURE; GENETICS; HUMAN; METABOLISM; MITOCHONDRION; PRION; SIGNAL TRANSDUCTION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; DEAD-BOX RNA HELICASES; HUMANS; MITOCHONDRIA; MODELS, MOLECULAR; PRIONS; RECOMBINANT PROTEINS; SIGNAL TRANSDUCTION; UBIQUITIN;

EID: 82655172367     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2011.155     Document Type: Article

References (15)

1. Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 2005;122:669-682. (Pubitemid 41242633)
2. Dixit E, Boulant S, Zhang Y, et al. Peroxisomes are signaling platforms for antiviral innate immunity. Cell 2010;141:668-681.
3. Tang ED, Wang CY. MAVS self-association mediates antiviral innate immune signaling. J Virol 2009;83:3420-3428.
4. Sun Q, Sun L, Liu HH, et al. The specific and essential role of MAVS in antiviral innate immune responses. Immunity 2006;24:633-642. (Pubitemid 43728147)
5. Kumar H, Kawai T, Kato H, et al. Essential role of IPS-1 in innate immune responses against RNA viruses. J Exp Med 2006;203:1795-1803. (Pubitemid 44036284)
6. Zeng W, Sun L, Jiang X, et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 2010;141:315-330.
7. Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 2011;146:448-461.
8. Tuite MF, Serio TR. The prion hypothesis: from biological anomaly to basic regulatory mechanism. Nat Rev Mol Cell Biol 2010;11:823-833.
9. Si K, Choi YB, White-Grindley E, Majumdar A, Kandel ER. Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to longterm facilitation. Cell 2010;140:421-435.
10. Wickner RB, Edskes HK, Kryndushkin D, McGlinchey R, Bateman D, Kelly A. Prion diseases of yeast: Amyloid structure and biology. Semin Cell Dev Biol 2011 February 21; doi:10.1016/j. semcdb.2011.02.021
11. Roberts BT, Wickner RB. Heritable activity: a prion that propagates by covalent autoactivation. Genes Dev 2003;17:2083-2087. (Pubitemid 37052288)
12. Goold R, Rabbanian S, Sutton L, et al. Rapid cell-surface prion protein conversion revealed using a novel cell system. Nat Commun 2011;2:281.
13. You F, Sun H, Zhou X, et al. PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. Nat Immunol 2009;10:1300-1308.
14. Lin SC, Lo YC, Wu H. Helical assembly in the MyD88-IRAK4-IRAK2 complex in TLR/IL-1R signalling. Nature 2010;465:885-890.
15. Potter JA, Randall RE, Taylor GL. Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain. BMC Struct Biol 2008;8:11.