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{{Infobox gene}}
{{Infobox gene}}
'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[RIG-I-like receptor]] [[DsRNA#Double-stranded RNA|dsRNA]] [[helicase]] [[enzyme]] that is encoded (in humans) by the ''DDX58'' [[gene]].  RIG-I is part of the [[RIG-I-like receptor]] family, which also includes [[MDA5]] and [[LGP2]], and functions as a [[pattern recognition receptor]] that is a sensor for viruses such as [[influenza A]], [[Sendai virus]], and [[flavivirus]].  Certain retroviruses, such as HIV-1, encode a protease that directs RIG-I to the lysosome for degradation, and thereby evade RIG-I mediated signaling.<ref>{{cite journal | vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J | title = RIG-I-mediated antiviral signaling is inhibited in HIV-1 infection by a protease-mediated sequestration of RIG-I | journal = Journal of Virology | volume = 85 | issue = 3 | pages = 1224–36 | date = Feb 2011 | pmc = 3020501 | doi = 10.1128/JVI.01635-10 | pmid = 21084468 }}</ref>  RIG-I typically recognizes short (< 4000nt) [[Directionality (molecular biology)|5′]] [[Polyphosphate|triphosphate]] uncapped double stranded or single stranded RNA.<ref>{{cite journal | vauthors = Pichlmair A, Schulz O, Tan CP, Näslund TI, Liljeström P, Weber F, Reis e Sousa C | title = RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates | journal = Science | volume = 314 | issue = 5801 | pages = 997–1001 | date = Nov 2006 | pmid = 17038589 | doi = 10.1126/science.1132998 }}</ref><ref>{{cite journal | vauthors = Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, Akira S, Fujita T | title = The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses | journal = Nature Immunology | volume = 5 | issue = 7 | pages = 730–7 | date = Jul 2004 | pmid = 15208624 | doi = 10.1038/ni1087 }}</ref><ref name="pmid18591409">{{cite journal | vauthors = Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, Hiiragi A, Dermody TS, Fujita T, Akira S | title = Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5 | journal = The Journal of Experimental Medicine | volume = 205 | issue = 7 | pages = 1601–10 | date = Jul 2008 | pmid = 18591409 | pmc = 2442638 | doi = 10.1084/jem.20080091 }}</ref> RIG-I and MDA5 are involved in activating [[VISA (gene)|MAVS]] and triggering an antiviral response.<ref>{{cite journal | vauthors = Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ | title = MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response | journal = Cell | volume = 146 | issue = 3 | pages = 448–61 | date = Aug 2011 | pmid = 21782231 | pmc = 3179916 | doi = 10.1016/j.cell.2011.06.041 }}</ref> RIG-I is also able to detect non-self 5′-triphosphorylated dsRNA transcribed from AT-rich dsDNA by DNA-dependent RNA polymerase III (Pol III). For many viruses, effective RIG-I-mediated antiviral responses are dependent on functionally active LGP2.<ref name="Satoh_2010">{{cite journal | vauthors = Satoh T, Kato H, Kumagai Y, Yoneyama M, Sato S, Matsushita K, Tsujimura T, Fujita T, Akira S, Takeuchi O | title = LGP2 is a positive regulator of RIG-I- and MDA5-mediated antiviral responses | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 4 | pages = 1512–7 | date = Jan 2010 | pmid = 20080593 | pmc = 2824407 | doi = 10.1073/pnas.0912986107 }}</ref>
'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[RIG-I-like receptor]] [[DsRNA#Double-stranded RNA|dsRNA]] [[helicase]] [[enzyme]] that is encoded (in humans) by the ''DDX58'' [[gene]].  RIG-I is part of the [[RIG-I-like receptor]] family, which also includes [[MDA5]] and [[LGP2]], and functions as a [[pattern recognition receptor]] that is a sensor for viruses such as [[influenza A]], [[Sendai virus]], and [[flavivirus]].  Certain retroviruses, such as HIV-1, encode a protease that directs RIG-I to the lysosome for degradation, and thereby evade RIG-I mediated signaling.<ref>{{cite journal | vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J | title = RIG-I-mediated antiviral signaling is inhibited in HIV-1 infection by a protease-mediated sequestration of RIG-I | journal = Journal of Virology | volume = 85 | issue = 3 | pages = 1224–36 | date = Feb 2011 | pmc = 3020501 | doi = 10.1128/JVI.01635-10 | pmid = 21084468 }}</ref>  RIG-I typically recognizes short (< 4000 nt) [[Directionality (molecular biology)|5′]] [[Polyphosphate|triphosphate]] uncapped double stranded or single stranded RNA.<ref>{{cite journal | vauthors = Pichlmair A, Schulz O, Tan CP, Näslund TI, Liljeström P, Weber F, Reis e Sousa C | title = RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates | journal = Science | volume = 314 | issue = 5801 | pages = 997–1001 | date = Nov 2006 | pmid = 17038589 | doi = 10.1126/science.1132998 }}</ref><ref>{{cite journal | vauthors = Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, Akira S, Fujita T | title = The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses | journal = Nature Immunology | volume = 5 | issue = 7 | pages = 730–7 | date = Jul 2004 | pmid = 15208624 | doi = 10.1038/ni1087 }}</ref><ref name="pmid18591409">{{cite journal | vauthors = Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, Hiiragi A, Dermody TS, Fujita T, Akira S | title = Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5 | journal = The Journal of Experimental Medicine | volume = 205 | issue = 7 | pages = 1601–10 | date = Jul 2008 | pmid = 18591409 | pmc = 2442638 | doi = 10.1084/jem.20080091 }}</ref> RIG-I and MDA5 are involved in activating [[VISA (gene)|MAVS]] and triggering an antiviral response.<ref>{{cite journal | vauthors = Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ | title = MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response | journal = Cell | volume = 146 | issue = 3 | pages = 448–61 | date = Aug 2011 | pmid = 21782231 | pmc = 3179916 | doi = 10.1016/j.cell.2011.06.041 }}</ref> RIG-I is also able to detect non-self 5′-triphosphorylated dsRNA transcribed from AT-rich dsDNA by DNA-dependent RNA polymerase III (Pol III). For many viruses, effective RIG-I-mediated antiviral responses are dependent on functionally active LGP2.<ref name="Satoh_2010">{{cite journal | vauthors = Satoh T, Kato H, Kumagai Y, Yoneyama M, Sato S, Matsushita K, Tsujimura T, Fujita T, Akira S, Takeuchi O | title = LGP2 is a positive regulator of RIG-I- and MDA5-mediated antiviral responses | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 4 | pages = 1512–7 | date = Jan 2010 | pmid = 20080593 | pmc = 2824407 | doi = 10.1073/pnas.0912986107 }}</ref>


== Function ==
== Function ==
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* {{cite journal | vauthors = Bowie AG, Fitzgerald KA | title = RIG-I: tri-ing to discriminate between self and non-self RNA | journal = Trends in Immunology | volume = 28 | issue = 4 | pages = 147–50 | date = Apr 2007 | pmid = 17307033 | doi = 10.1016/j.it.2007.02.002 }}
* {{cite journal | vauthors = Bowie AG, Fitzgerald KA | title = RIG-I: tri-ing to discriminate between self and non-self RNA | journal = Trends in Immunology | volume = 28 | issue = 4 | pages = 147–50 | date = Apr 2007 | pmid = 17307033 | doi = 10.1016/j.it.2007.02.002 }}
* {{cite journal | vauthors = Imaizumi T, Aratani S, Nakajima T, Carlson M, Matsumiya T, Tanji K, Ookawa K, Yoshida H, Tsuchida S, McIntyre TM, Prescott SM, Zimmerman GA, Satoh K | title = Retinoic acid-inducible gene-I is induced in endothelial cells by LPS and regulates expression of COX-2 | journal = Biochemical and Biophysical Research Communications | volume = 292 | issue = 1 | pages = 274–9 | date = Mar 2002 | pmid = 11890704 | doi = 10.1006/bbrc.2002.6650 }}
* {{cite journal | vauthors = Imaizumi T, Aratani S, Nakajima T, Carlson M, Matsumiya T, Tanji K, Ookawa K, Yoshida H, Tsuchida S, McIntyre TM, Prescott SM, Zimmerman GA, Satoh K | title = Retinoic acid-inducible gene-I is induced in endothelial cells by LPS and regulates expression of COX-2 | journal = Biochemical and Biophysical Research Communications | volume = 292 | issue = 1 | pages = 274–9 | date = Mar 2002 | pmid = 11890704 | doi = 10.1006/bbrc.2002.6650 }}
* {{cite journal | vauthors = Cui XF, Imaizumi T, Yoshida H, Borden EC, Satoh K | title = Retinoic acid-inducible gene-I is induced by interferon-gamma and regulates the expression of interferon-gamma stimulated gene 15 in MCF-7 cells | journal = Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire | volume = 82 | issue = 3 | pages = 401–5 | date = Jun 2004 | pmid = 15181474 | doi = 10.1139/o04-041 }}
* {{cite journal | vauthors = Cui XF, Imaizumi T, Yoshida H, Borden EC, Satoh K | title = Retinoic acid-inducible gene-I is induced by interferon-gamma and regulates the expression of interferon-gamma stimulated gene 15 in MCF-7 cells | journal = Biochemistry and Cell Biology | volume = 82 | issue = 3 | pages = 401–5 | date = Jun 2004 | pmid = 15181474 | doi = 10.1139/o04-041 }}
* {{cite journal | vauthors = Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, Akira S, Fujita T | title = The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses | journal = Nature Immunology | volume = 5 | issue = 7 | pages = 730–7 | date = Jul 2004 | pmid = 15208624 | doi = 10.1038/ni1087 }}
* {{cite journal | vauthors = Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, Akira S, Fujita T | title = The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses | journal = Nature Immunology | volume = 5 | issue = 7 | pages = 730–7 | date = Jul 2004 | pmid = 15208624 | doi = 10.1038/ni1087 }}
* {{cite journal | vauthors = Imaizumi T, Yagihashi N, Hatakeyama M, Yamashita K, Ishikawa A, Taima K, Yoshida H, Inoue I, Fujita T, Yagihashi S, Satoh K | title = Expression of retinoic acid-inducible gene-I in vascular smooth muscle cells stimulated with interferon-gamma | journal = Life Sciences | volume = 75 | issue = 10 | pages = 1171–80 | date = Jul 2004 | pmid = 15219805 | doi = 10.1016/j.lfs.2004.01.030 }}
* {{cite journal | vauthors = Imaizumi T, Yagihashi N, Hatakeyama M, Yamashita K, Ishikawa A, Taima K, Yoshida H, Inoue I, Fujita T, Yagihashi S, Satoh K | title = Expression of retinoic acid-inducible gene-I in vascular smooth muscle cells stimulated with interferon-gamma | journal = Life Sciences | volume = 75 | issue = 10 | pages = 1171–80 | date = Jul 2004 | pmid = 15219805 | doi = 10.1016/j.lfs.2004.01.030 }}

Latest revision as of 07:32, 10 January 2019

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Identifiers
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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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RefSeq (mRNA)

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RefSeq (protein)

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RIG-I (retinoic acid-inducible gene I) is a RIG-I-like receptor dsRNA helicase enzyme that is encoded (in humans) by the DDX58 gene. RIG-I is part of the RIG-I-like receptor family, which also includes MDA5 and LGP2, and functions as a pattern recognition receptor that is a sensor for viruses such as influenza A, Sendai virus, and flavivirus. Certain retroviruses, such as HIV-1, encode a protease that directs RIG-I to the lysosome for degradation, and thereby evade RIG-I mediated signaling.[1] RIG-I typically recognizes short (< 4000 nt) 5′ triphosphate uncapped double stranded or single stranded RNA.[2][3][4] RIG-I and MDA5 are involved in activating MAVS and triggering an antiviral response.[5] RIG-I is also able to detect non-self 5′-triphosphorylated dsRNA transcribed from AT-rich dsDNA by DNA-dependent RNA polymerase III (Pol III). For many viruses, effective RIG-I-mediated antiviral responses are dependent on functionally active LGP2.[6]

Function

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. RIG-I contains a RNA helicase-DEAD box motifs and a caspase recruitment domain (CARD). RIG-I is involved in viral double-stranded (ds) RNA recognition and the regulation of immune response.[7]

References

  1. ↑ Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J (Feb 2011). "RIG-I-mediated antiviral signaling is inhibited in HIV-1 infection by a protease-mediated sequestration of RIG-I". Journal of Virology. 85 (3): 1224–36. doi:10.1128/JVI.01635-10. PMC 3020501. PMID 21084468.
  2. ↑ Pichlmair A, Schulz O, Tan CP, Näslund TI, Liljeström P, Weber F, Reis e Sousa C (Nov 2006). "RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates". Science. 314 (5801): 997–1001. doi:10.1126/science.1132998. PMID 17038589.
  3. ↑ Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, Akira S, Fujita T (Jul 2004). "The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses". Nature Immunology. 5 (7): 730–7. doi:10.1038/ni1087. PMID 15208624.
  4. ↑ Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, Hiiragi A, Dermody TS, Fujita T, Akira S (Jul 2008). "Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5". The Journal of Experimental Medicine. 205 (7): 1601–10. doi:10.1084/jem.20080091. PMC 2442638. PMID 18591409.
  5. ↑ Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ (Aug 2011). "MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response". Cell. 146 (3): 448–61. doi:10.1016/j.cell.2011.06.041. PMC 3179916. PMID 21782231.
  6. ↑ Satoh T, Kato H, Kumagai Y, Yoneyama M, Sato S, Matsushita K, Tsujimura T, Fujita T, Akira S, Takeuchi O (Jan 2010). "LGP2 is a positive regulator of RIG-I- and MDA5-mediated antiviral responses". Proceedings of the National Academy of Sciences of the United States of America. 107 (4): 1512–7. doi:10.1073/pnas.0912986107. PMC 2824407. PMID 20080593.
  7. ↑ "Entrez Gene: DDX58 DEAD (Asp-Glu-Ala-Asp) box polypeptide 58".

Further reading

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