RIG-I - Revision history

167.98.155.165: /* Further reading */ Category

2024-08-27T16:57:08Z

Innatestability: /* Identification and naming */

2024-05-24T13:19:53Z

Identification and naming

← Previous revision		Revision as of 13:19, 24 May 2024
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	Usually, RIG-I recognizes foreign RNA. However, it can sometimes recognize "self" RNAs. RIG-I has been shown to enable [[breast cancer]] cells (BrCa) to resist treatments and grow because of an IFN response to noncoding RNA. In contrast, RIG-I in other types of cancer, such as acute [[myeloid leukemia]] and [[hepatocellular carcinoma]], can act as a tumor suppressor.<ref name="Xu_2018" /> If cancer causing viruses infect a cell, however, RIG-I can lead to cell death. Cell death can occur via [[apoptosis]] via the [[Caspase 3\|caspase-3]] pathway, or through IFN-dependent T cells and [[natural killer cell]]s.<ref>{{cite journal \| vauthors = Żeromski J, Kaczmarek M, Boruczkowski M, Kierepa A, Kowala-Piaskowska A, Mozer-Lisewska I \| title = Significance and Role of Pattern Recognition Receptors in Malignancy \| journal = Archivum Immunologiae et Therapiae Experimentalis \| volume = 67 \| issue = 3 \| pages = 133–141 \| date = June 2019 \| pmid = 30976817 \| pmc = 6509067 \| doi = 10.1007/s00005-019-00540-x }}</ref>		Usually, RIG-I recognizes foreign RNA. However, it can sometimes recognize "self" RNAs. RIG-I has been shown to enable [[breast cancer]] cells (BrCa) to resist treatments and grow because of an IFN response to noncoding RNA. In contrast, RIG-I in other types of cancer, such as acute [[myeloid leukemia]] and [[hepatocellular carcinoma]], can act as a tumor suppressor.<ref name="Xu_2018" /> If cancer causing viruses infect a cell, however, RIG-I can lead to cell death. Cell death can occur via [[apoptosis]] via the [[Caspase 3\|caspase-3]] pathway, or through IFN-dependent T cells and [[natural killer cell]]s.<ref>{{cite journal \| vauthors = Żeromski J, Kaczmarek M, Boruczkowski M, Kierepa A, Kowala-Piaskowska A, Mozer-Lisewska I \| title = Significance and Role of Pattern Recognition Receptors in Malignancy \| journal = Archivum Immunologiae et Therapiae Experimentalis \| volume = 67 \| issue = 3 \| pages = 133–141 \| date = June 2019 \| pmid = 30976817 \| pmc = 6509067 \| doi = 10.1007/s00005-019-00540-x }}</ref>

	== Identification and ~~naming~~ ==		== Identification and Naming ==
	In 2000, RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| doi-access = free }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.		In 2000, RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| doi-access = free }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.

Innatestability: /* Identification and naming */

2024-04-02T09:22:07Z

Identification and naming

← Previous revision		Revision as of 09:22, 2 April 2024
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	== Identification and naming ==		== Identification and naming ==
	RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| doi-access = free }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.		In 2000, RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| doi-access = free }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.

	== References ==		== References ==

Innatestability: removed "blunt 5' end" which was confusing and reads like 5' ends without phosphate could be recognized by RIG-I. Reference 7 (Goubau et al.) show that CIP treatment substantially reduces RIG-I recognition. Similarly, 5' diP and triP activate RIG-I, while 5' monoP does not.

2024-02-16T14:31:36Z

removed "blunt 5' end" which was confusing and reads like 5' ends without phosphate could be recognized by RIG-I. Reference 7 (Goubau et al.) show that CIP treatment substantially reduces RIG-I recognition. Similarly, 5' diP and triP activate RIG-I, while 5' monoP does not.

← Previous revision		Revision as of 14:31, 16 February 2024
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	'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>		'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>

	RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a ~~blunt 5' end,~~ 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1).<ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref> These are often generated during a viral infection but can also be host-derived.<ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref> Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />		RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1).<ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref> These are often generated during a viral infection but can also be host-derived.<ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref> Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />

	Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]].<ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>		Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]].<ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>

Citation bot: Removed proxy/dead URL that duplicated identifier. | Use this bot. Report bugs. | Suggested by Whoop whoop pull up | #UCB_webform 117/1025

2023-11-15T21:12:34Z

Removed proxy/dead URL that duplicated identifier. | Use this bot. Report bugs. | Suggested by Whoop whoop pull up | #UCB_webform 117/1025

← Previous revision		Revision as of 21:12, 15 November 2023
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	== Identification and naming ==		== Identification and naming ==
	RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 ~~\| url = https://pubmed.ncbi.nlm.nih.gov/10942397/~~ \| doi-access = free }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.		RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| doi-access = free }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.

	== References ==		== References ==

OAbot: Open access bot: doi added to citation with #oabot.

2023-08-12T23:13:40Z

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← Previous revision		Revision as of 23:13, 12 August 2023
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	== Identification and naming ==		== Identification and naming ==
	RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| url = https://pubmed.ncbi.nlm.nih.gov/10942397/ }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.		RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| url = https://pubmed.ncbi.nlm.nih.gov/10942397/ \| doi-access = free }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.

	== References ==		== References ==

JCW-CleanerBot: clean up, removed: = Biochimie et Biologie Cellulaire

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← Previous revision		Revision as of 19:30, 5 August 2023
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	{{Short description\|Mammalian protein found in humans}}		{{Short description\|Mammalian protein found in humans}}
	{{Infobox gene}}		{{Infobox gene}}
	'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>		'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>

	RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a blunt 5' end, 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1) <ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref>. These are often generated during a viral infection but can also be host-derived <ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref>. Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />		RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a blunt 5' end, 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1).<ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref> These are often generated during a viral infection but can also be host-derived.<ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref> Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />

	Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]]. <ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>		Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]].<ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>

	== Structure ==		== Structure ==
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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 = 147–150 \| date = April 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 = 147–150 \| date = April 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 \| display-authors = 6 \| 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 = 274–279 \| date = March 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 \| display-authors = 6 \| 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 = 274–279 \| date = March 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 = 401–405 \| date = June 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 = 401–405 \| date = June 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 \| display-authors = 6 \| 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 = 730–737 \| date = July 2004 \| pmid = 15208624 \| doi = 10.1038/ni1087 \| s2cid = 34876422 }}		* {{cite journal \| vauthors = Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, Akira S, Fujita T \| display-authors = 6 \| 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 = 730–737 \| date = July 2004 \| pmid = 15208624 \| doi = 10.1038/ni1087 \| s2cid = 34876422 }}
	* {{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 \| display-authors = 6 \| 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 = 1171–1180 \| date = July 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 \| display-authors = 6 \| 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 = 1171–1180 \| date = July 2004 \| pmid = 15219805 \| doi = 10.1016/j.lfs.2004.01.030 }}

Innatestability: /* Identification and naming */

2023-08-04T14:55:23Z

Identification and naming

← Previous revision		Revision as of 14:55, 4 August 2023
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	== Identification and naming ==		== Identification and naming ==
	RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| url = https://pubmed.ncbi.nlm.nih.gov/10942397/ }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization.		RIG-I was named by researchers from the Shanghai Institute of Hematology who identified novel genes that respond to [[Tretinoin\|all-''trans'' retinoic acid]] (ATRA) in leukemia cells.<ref>{{cite journal \| vauthors = Liu TX, Zhang JW, Tao J, Zhang RB, Zhang QH, Zhao CJ, Tong JH, Lanotte M, Waxman S, Chen SJ, Mao M, Hu GX, Zhu L, Chen Z \| display-authors = 6 \| title = Gene expression networks underlying retinoic acid-induced differentiation of acute promyelocytic leukemia cells \| journal = Blood \| volume = 96 \| issue = 4 \| pages = 1496–1504 \| date = August 2000 \| doi = 10.1182/blood.V96.4.1496 \| pmid = 10942397 \| url = https://pubmed.ncbi.nlm.nih.gov/10942397/ }}</ref> RIG-I and the other genes were assigned the temporary name of RIG (retinoic acid–induced gene) in the format of RIG-A, RIG-B etc by the group, however they performed no additional characterization on RIG-I.

	== References ==		== References ==

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2023-07-28T14:03:21Z

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2023-07-28T14:00:12Z

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← Previous revision		Revision as of 16:57, 27 August 2024
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	Note: RARRES3 (Gene ID: 5920) and DDX58 (Gene ID: 23586) share the RIG1/RIG-1 alias in common. RIG1 is a widely used alternative name for DExD/H-box helicase 58 (DDX58), which can be confused with the retinoic acid receptor responder 3 (RARRES3) gene, since they share the same alias. [22 Jan 2019]		Note: RARRES3 (Gene ID: 5920) and DDX58 (Gene ID: 23586) share the RIG1/RIG-1 alias in common. RIG1 is a widely used alternative name for DExD/H-box helicase 58 (DDX58), which can be confused with the retinoic acid receptor responder 3 (RARRES3) gene, since they share the same alias. [22 Jan 2019]

			[[Category:Helicases]]
	[[Category:RIG-I-like receptors]]		[[Category:RIG-I-like receptors]]
	[[Category:Intracellular receptors]]		[[Category:Intracellular receptors]]

← Previous revision		Revision as of 14:31, 16 February 2024
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	'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>		'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>

	RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a ~~blunt 5' end,~~ 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1).<ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref> These are often generated during a viral infection but can also be host-derived.<ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref> Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />		RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1).<ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref> These are often generated during a viral infection but can also be host-derived.<ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref> Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />

	Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]].<ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>		Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]].<ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>

← Previous revision		Revision as of 19:30, 5 August 2023
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	{{Short description\|Mammalian protein found in humans}}		{{Short description\|Mammalian protein found in humans}}
	{{Infobox gene}}		{{Infobox gene}}
	'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>		'''RIG-I''' ('''retinoic acid-inducible gene I''') is a [[cytosol]]ic [[pattern recognition receptor]] (PRR) that can mediate induction of a [[Interferon type I\|type-I interferon]] (IFN1) response.<ref name="Kell_2015">{{cite journal \| vauthors = Kell AM, Gale M \| title = RIG-I in RNA virus recognition \| journal = Virology \| volume = 479-480 \| pages = 110–121 \| date = May 2015 \| pmid = 25749629 \| pmc = 4424084 \| doi = 10.1016/j.virol.2015.02.017 }}</ref> RIG-I is an essential molecule in the [[innate immune system]] for recognizing cells that have been infected with a virus. These viruses can include [[West Nile virus]], [[Japanese encephalitis\|Japanese Encephalitis virus]], [[influenza A]], [[Sendai virus]], [[flavivirus]], and [[coronavirus]]es.<ref name="Kell_2015" /><ref name="Solis_2011">{{cite journal \| vauthors = Solis M, Nakhaei P, Jalalirad M, Lacoste J, Douville R, Arguello M, Zhao T, Laughrea M, Wainberg MA, Hiscott J \| display-authors = 6 \| 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 = 1224–1236 \| date = February 2011 \| pmid = 21084468 \| pmc = 3020501 \| doi = 10.1128/JVI.01635-10 }}</ref>

	RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a blunt 5' end, 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1) <ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref>. These are often generated during a viral infection but can also be host-derived <ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref>. Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />		RIG-I is an ATP-dependent [[DExD/H box proteins\|DExD/H box]] [[RNA Helicase\|RNA helicase]] that is activated by immunostimulatory RNAs from viruses as well as RNAs of other origins. RIG-I recognizes short [[double-stranded RNA]] (dsRNA) in the cytosol with a blunt 5' end, 5' tri- or di-phosphate end or a [[Five-prime cap\|5' 7-methyl guanosine (m7G) cap]] (cap-0), but not RNA with a 5' m7G cap having a ribose 2′-O-methyl modification (cap-1).<ref>{{cite journal \| vauthors = Goubau D, Schlee M, Deddouche S, Pruijssers AJ, Zillinger T, Goldeck M, Schuberth C, Van der Veen AG, Fujimura T, Rehwinkel J, Iskarpatyoti JA, Barchet W, Ludwig J, Dermody TS, Hartmann G, Reis e Sousa C \| display-authors = 6 \| title = Antiviral immunity via RIG-I-mediated recognition of RNA bearing 5'-diphosphates \| journal = Nature \| volume = 514 \| issue = 7522 \| pages = 372–375 \| date = October 2014 \| pmid = 25119032 \| pmc = 4201573 \| doi = 10.1038/nature13590 \| bibcode = 2014Natur.514..372G }}</ref><ref>{{cite journal \| vauthors = Devarkar SC, Wang C, Miller MT, Ramanathan A, Jiang F, Khan AG, Patel SS, Marcotrigiano J \| display-authors = 6 \| title = Structural basis for m7G recognition and 2'-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I \| journal = Proceedings of the National Academy of Sciences of the United States of America \| volume = 113 \| issue = 3 \| pages = 596–601 \| date = January 2016 \| pmid = 26733676 \| doi = 10.1073/pnas.1515152113 \| pmc = 4725518 \| bibcode = 2016PNAS..113..596D \| doi-access = free }}</ref> These are often generated during a viral infection but can also be host-derived.<ref name="Kell_2015" /><ref name="Brisse_2019">{{cite journal \| vauthors = Brisse M, Ly H \| title = Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 \| language = English \| journal = Frontiers in Immunology \| volume = 10 \| pages = 1586 \| date = 2019 \| pmid = 31379819 \| pmc = 6652118 \| doi = 10.3389/fimmu.2019.01586 \| doi-access = free }}</ref><ref name="Xu_2018">{{cite journal \| vauthors = Xu XX, Wan H, Nie L, Shao T, Xiang LX, Shao JZ \| title = RIG-I: a multifunctional protein beyond a pattern recognition receptor \| journal = Protein & Cell \| volume = 9 \| issue = 3 \| pages = 246–253 \| date = March 2018 \| pmid = 28593618 \| pmc = 5829270 \| doi = 10.1007/s13238-017-0431-5 }}</ref><ref>{{cite journal \| vauthors = Chiang JJ, Sparrer KM, van Gent M, Lässig C, Huang T, Osterrieder N, Hopfner KP, Gack MU \| display-authors = 6 \| title = Viral unmasking of cellular 5S rRNA pseudogene transcripts induces RIG-I-mediated immunity \| journal = Nature Immunology \| volume = 19 \| issue = 1 \| pages = 53–62 \| date = January 2018 \| pmid = 29180807 \| pmc = 5815369 \| doi = 10.1038/s41590-017-0005-y }}</ref><ref>{{cite journal \| vauthors = Zhao Y, Ye X, Dunker W, Song Y, Karijolich J \| title = RIG-I like receptor sensing of host RNAs facilitates the cell-intrinsic immune response to KSHV infection \| journal = Nature Communications \| volume = 9 \| issue = 1 \| pages = 4841 \| date = November 2018 \| pmid = 30451863 \| pmc = 6242832 \| doi = 10.1038/s41467-018-07314-7 \| bibcode = 2018NatCo...9.4841Z }}</ref> Once activated by the dsRNA, the N-terminus [[CARD domain\|caspase activation and recruitment domains]] (CARDs) migrate and bind with CARDs attached to mitochondrial antiviral signaling protein ([[MAVS (gene)\|MAVS]]) to activate the signaling pathway for IFN1.<ref name="Kell_2015" /><ref name="Brisse_2019" />

	Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]]. <ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>		Type-I IFNs have three main functions: to limit the virus from spreading to nearby cells, promote an innate immune response, including inflammatory responses, and help activate the [[adaptive immune system]].<ref name="Ivashkiv_2014">{{cite journal \| vauthors = Ivashkiv LB, Donlin LT \| title = Regulation of type I interferon responses \| journal = Nature Reviews. Immunology \| volume = 14 \| issue = 1 \| pages = 36–49 \| date = January 2014 \| pmid = 24362405 \| pmc = 4084561 \| doi = 10.1038/nri3581 }}</ref> Other studies have shown that in different microenvironments, such as in cancerous cells, RIG-I has more functions other than viral recognition.<ref name="Xu_2018" /> RIG-I orthologs are found in mammals, geese, ducks, some fish, and some reptiles.<ref name="Brisse_2019" /> RIG-I is in most cells, including various innate immune system cells, and is usually in an inactive state.<ref name="Kell_2015" /><ref name="Brisse_2019" /> [[Knockout mouse\|Knockout mice]] that have been designed to have a deleted or non-functioning RIG-I gene are not healthy and typically die embryonically. If they survive, the mice have serious developmental dysfunction.<ref name="Brisse_2019" /> The stimulator of interferon genes [[STING]] antagonizes RIG-I by binding its N-terminus, probably as to avoid overactivation of RIG-I signaling and the associated [[autoimmunity]].<ref>{{cite journal \| vauthors = Yu P, Miao Z, Li Y, Bansal R, Peppelenbosch MP, Pan Q \| title = cGAS-STING effectively restricts murine norovirus infection but antagonizes the antiviral action of N-terminus of RIG-I in mouse macrophages \| journal = Gut Microbes \| volume = 13 \| issue = 1 \| pages = 1959839 \| date = January 2021 \| pmid = 34347572 \| pmc = 8344765 \| doi = 10.1080/19490976.2021.1959839 }}</ref>

	== Structure ==		== Structure ==
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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 = 147–150 \| date = April 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 = 147–150 \| date = April 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 \| display-authors = 6 \| 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 = 274–279 \| date = March 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 \| display-authors = 6 \| 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 = 274–279 \| date = March 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 = 401–405 \| date = June 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 = 401–405 \| date = June 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 \| display-authors = 6 \| 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 = 730–737 \| date = July 2004 \| pmid = 15208624 \| doi = 10.1038/ni1087 \| s2cid = 34876422 }}		* {{cite journal \| vauthors = Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, Akira S, Fujita T \| display-authors = 6 \| 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 = 730–737 \| date = July 2004 \| pmid = 15208624 \| doi = 10.1038/ni1087 \| s2cid = 34876422 }}
	* {{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 \| display-authors = 6 \| 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 = 1171–1180 \| date = July 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 \| display-authors = 6 \| 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 = 1171–1180 \| date = July 2004 \| pmid = 15219805 \| doi = 10.1016/j.lfs.2004.01.030 }}