View source for Stimulator of interferon genes

{{Short description|Protein-coding gene in the species Homo sapiens}}
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{{Redirect|MITA|the Maine Island Trail Association|Maine Island Trail Association}}{{Infobox gene}}
'''Stimulator of interferon genes''' ('''STING'''), also known as '''transmembrane protein 173''' ('''TMEM173''') and '''MPYS'''/'''MITA'''/'''ERIS''' is a [[protein]] that in humans is encoded by the STING1 [[gene]].<ref name="entrez">{{cite web | title = STING1 stimulator of interferon response cGAMP interactor 1 [ Homo sapiens (human) ]| url = https://www.ncbi.nlm.nih.gov/gene/340061}}</ref>
STING plays an important role in [[Innate immune system|innate immunity]]. STING induces [[Interferon type I|type I interferon]] production when cells are infected with intracellular pathogens, such as [[viruses]], [[mycobacteria]] and [[parasite|intracellular parasites]].<ref name="pmid20022884">{{cite journal | vauthors = Nakhaei P, Hiscott J, Lin R | title = STING-ing the antiviral pathway | journal = Journal of Molecular Cell Biology | volume = 2 | issue = 3 | pages = 110–2 | date = Jun 2010 | pmid = 20022884 | doi = 10.1093/jmcb/mjp048 | doi-access = free }}</ref> [[Interferon type I|Type I interferon]], mediated by STING, protects infected cells and nearby cells from local infection by binding to the same cell that secretes it ([[autocrine]] signaling) and nearby cells ([[paracrine]] signaling.) It thus plays an important role, for instance, in controlling [[norovirus]] infection.<ref name="pmid34347572">{{cite journal | vauthors = NYu 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 macrophage | journal = Gut Microbes | volume = 13 | issue = 1 | pages = 1959839 | date =  2021 | pmid = 34347572 | pmc = 8344765 | doi = 10.1080/19490976.2021.1959839|issn=1949-0976 | doi-access = free }}</ref>
STING works as both a direct [[The cGAS – STING cytosolic DNA sensing pathway|cytosolic DNA sensor]] (CDS) and an [[Signal transducing adaptor protein|adaptor protein]] in [[Interferon type I|Type I interferon]] signaling through different molecular mechanisms. It has been shown to activate downstream transcription factors [[STAT6]] and [[IRF3]] through [[TANK-binding kinase 1|TBK1]], which are responsible for antiviral response and innate immune response against [[Intracellular parasite|intracellular pathogen]].<ref name="pmid23238760" />
== Structure ==
[[File:HSTING protein architecture.png|thumb|350px|Human STING Protein Architecture]]
Amino acids 1–379 of human STING include the 4 [[Transmembrane region#Transmembrane domain|transmembrane regions]] (TMs) and a [[C-terminus#C-terminal domain|C-terminal domain]]. The [[C-terminus#C-terminal domain|C-terminal domain]] (CTD: amino acids 138–379) contains the dimerization domain (DD) and the [[C-terminus|carboxy-terminal tail]] (CTT: amino acids 340–379).<ref name="pmid23238760">{{cite journal | vauthors = Burdette DL, Vance RE | title = STING and the innate immune response to nucleic acids in the cytosol | journal = Nature Immunology | volume = 14 | issue = 1 | pages = 19–26 | date = Jan 2013 | pmid = 23238760 | doi = 10.1038/ni.2491 | s2cid = 7968532 }}</ref>
The STING forms a symmetrical dimer in the cell. STING dimer resembles a butterfly, with a deep cleft between the two protomers. The [[hydrophobic]] residues from each STING protomer form [[hydrophobic interactions]] between each other at the interface.<ref name="pmid23238760" /><ref name="pmid22728658">{{cite journal | vauthors = Shu C, Yi G, Watts T, Kao CC, Li P | title = Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system | journal = Nature Structural & Molecular Biology | volume = 19 | issue = 7 | pages = 722–4 | date = Jul 2012 | pmid = 22728658 | pmc = 3392545 | doi = 10.1038/nsmb.2331 }}</ref>
== Expression ==
STING is expressed in [[hematopoietic]] cells in [[Lymphoid tissue#Lymphoid tissue|peripheral lymphoid tissues]], including [[T lymphocytes]], [[NK cells]], [[myeloid cells]] and [[monocytes]]. It has also been shown that STING is highly expressed in lung, [[ovary]], heart, [[smooth muscle]], [[retina]], [[bone marrow]] and vagina.<ref>{{cite web |url=http://biogps.org/#goto=genereport&id=72512 |title=EST expression profile of TMEM173 |website=biogps org |publisher=biogps.org}}</ref><ref>{{cite web |url=https://www.ncbi.nlm.nih.gov/geo/tools/profileGraph.cgi?ID=GDS1085:40762 |title=NCBI TMEM173 expression GEOprofile |website=NCBI |publisher=www.ncbi.nlm.nih.gov/geoprofiles}}</ref>
== Localization ==
The subcellular localization of STING has been elucidated as an [[endoplasmic reticulum]] protein. Also, it is likely that STING associates in close proximity with [[Mitochondrion#Mitochondria-associated ER membrane (MAM)|mitochondria associated ER membrane (MAM)]]-the interface between the mitochondrion and the ER.<ref name="pmid18724357">{{cite journal | vauthors = Ishikawa H, Barber GN | title = STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling | journal = Nature | volume = 455 | issue = 7213 | pages = 674–8 | date = Oct 2008 | pmid = 18724357 | pmc = 2804933 | doi = 10.1038/nature07317 | bibcode = 2008Natur.455..674I }}</ref> During intracellular infection, STING is able to relocalize from [[endoplasmic reticulum]] to [[Transport vesicle#Transport vesicles|perinuclear vesicles]] potentially involved in [[exocyst]] mediated transport.<ref name="pmid18724357" /> STING has also been shown to colocalize with autophagy proteins, [[MAP1LC3A|microtubule-associated protein 1 light chain 3 (LC3)]] and [[ATG9A|autophagy-related protein 9A]], after double-stranded DNA stimulation, suggesting its presence in the [[autophagy|autophagosome]].<ref name="pmid19926846">{{cite journal | vauthors = Saitoh T, Fujita N, Hayashi T, Takahara K, Satoh T, Lee H, Matsunaga K, Kageyama S, Omori H, Noda T, Yamamoto N, Kawai T, Ishii K, Takeuchi O, Yoshimori T, Akira S | title = Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 49 | pages = 20842–6 | date = Dec 2009 | pmid = 19926846 | pmc = 2791563 | doi = 10.1073/pnas.0911267106 | bibcode = 2009PNAS..10620842S | doi-access = free }}</ref>
== Function ==
STING mediates the [[Interferon type I|type I interferon]] production in response to intracellular DNA and a variety of intracellular pathogens, including [[viruses]], [[Intracellular parasite|intracellular bacteria]] and [[intracellular parasite]]s.<ref name="pmid21239155">{{cite journal | vauthors = Barber GN | title = Innate immune DNA sensing pathways: STING, AIMII and the regulation of interferon production and inflammatory responses | journal = Current Opinion in Immunology | volume = 23 | issue = 1 | pages = 10–20 | date = Feb 2011 | pmid = 21239155 | doi = 10.1016/j.coi.2010.12.015 | pmc=3881186}}</ref> Upon infection, STING from infected cells can sense the presence of [[nucleic acids]] from intracellular pathogens, and then induce [[Interferon type I#IFN-β|interferon β]] and more than 10 forms of [[Interferon type I#IFN-α|interferon α]] production. [[Interferon type I|Type I interferon]] produced by infected cells can find and bind to [[Interferon-alpha/beta receptor]] of nearby cells to protect cells from local infection.
=== Antiviral immunity ===
STING elicits powerful [[Interferon type I|type I interferon immunity]] against viral infection. After [[viral entry]], viral [[nucleic acids]] are present in the cytosol of infected cells. Several DNA sensors, such as [[ZBP1|DAI]], [[RNA polymerase III]], [[IFI16]], [[DDX41]] and [[Cyclic GMP-AMP synthase|cGAS]], can detect foreign [[nucleic acids]]. After recognizing viral DNA, DNA sensors initiate the downstream signaling pathways by activating STING-mediated interferon response.<ref name="pmid21940216">{{cite journal | vauthors = Keating SE, Baran M, Bowie AG | title = Cytosolic DNA sensors regulating type I interferon induction | journal = Trends in Immunology | volume = 32 | issue = 12 | pages = 574–81 | date = Dec 2011 | pmid = 21940216 | doi = 10.1016/j.it.2011.08.004 | hdl = 2262/68041 | url = http://www.tara.tcd.ie/bitstream/2262/68041/1/Keating%20DNA%20sensing%20TiI%20author%20version.pdf | hdl-access = free }}</ref>
''[[Adenoviridae|Adenovirus]]'', [[herpes simplex virus]], HSV-1 and HSV-2, as well as the [[RNA virus#Single-stranded RNA viruses and RNA Sense|negative-stranded RNA virus]], [[vesicular stomatitis virus]] (VSV), have been shown to be able to activate a STING-dependent [[innate immune response]].<ref name="pmid21239155" />
STING deficiency in mice led to lethal susceptibility to HSV-1 infection due to the lack of a successful type I interferon response.<ref>{{cite journal | vauthors = Ma Z, Damania B | title = The cGAS-STING Defense Pathway and Its Counteraction by Viruses | journal = Cell Host & Microbe | volume = 19 | issue = 2 | pages = 150–8 | date = February 2016 | pmid = 26867174 | pmc = 4755325 | doi = 10.1016/j.chom.2016.01.010 }}</ref>
Point mutation of [[serine]]-358 dampens STING-IFN activation in bats and is suggested to give bats their ability to serve as reservoir hosts.<ref>{{cite journal | vauthors = Xie J, Li Y, Shen X, Got G, Zhu Y, Cui J, Wang L, Shi Z, Zhou P | title = Dampened STING-Dependent Interferon Activation in Bats | journal = Cell Host & Microbe | volume = 23 | issue = 3 | pages = 297–301.e4 | date = March 2018 | doi = 10.1016/j.chom.2018.01.006 | pmid = 29478775 | pmc = 7104992 | doi-access = free }}</ref>
=== Against intracellular bacteria ===
Intracellular bacteria, ''[[Listeria monocytogenes]]'', have been shown to stimulate host immune response through STING.<ref name="pmid23378430">{{cite journal | vauthors = Jin L, Getahun A, Knowles HM, Mogan J, Akerlund LJ, Packard TA, Perraud AL, Cambier JC | title = STING/MPYS mediates host defense against Listeria monocytogenes infection by regulating Ly6C(hi) monocyte migration | journal = Journal of Immunology | volume = 190 | issue = 6 | pages = 2835–43 | date = Mar 2013 | pmid = 23378430 | doi = 10.4049/jimmunol.1201788 | pmc=3593745}}</ref> STING may play an important role in the production of [[MCP-1]] and [[CCL7]] chemokines. STING deficient monocytes are intrinsically defective in migration to the liver during ''[[Listeria monocytogenes]]'' infection. In this way, STING protects host from ''[[Listeria monocytogenes]]'' infection by regulating [[monocyte]] migration. The activation of STING is likely to be mediated by [[cyclic di-AMP]] secreted by intracellular bacteria.<ref name="pmid23378430" /><ref name="pmid20508090">{{cite journal | vauthors = Woodward JJ, Iavarone AT, Portnoy DA | title = c-di-AMP secreted by intracellular Listeria monocytogenes activates a host type I interferon response | journal = Science | volume = 328 | issue = 5986 | pages = 1703–5 | date = Jun 2010 | pmid = 20508090 | pmc = 3156580 | doi = 10.1126/science.1189801 | bibcode = 2010Sci...328.1703W }}</ref>
=== Other ===
STING may be an important molecule for protective immunity against infectious organisms. For example, animals that cannot express STING are more susceptible to infection from [[Vesicular stomatitis virus|VSV]], [[HSV-1]] and ''[[Listeria monocytogenes]]'', suggesting its potential correlation to human infectious diseases.<ref name="pmid19776740">{{cite journal | vauthors = Ishikawa H, Ma Z, Barber GN | title = STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity | journal = Nature | volume = 461 | issue = 7265 | pages = 788–92 | date = Oct 2009 | pmid = 19776740 | doi = 10.1038/nature08476 | pmc=4664154| bibcode = 2009Natur.461..788I }}</ref>
=== Role in host immunity ===
Although [[type I interferon|type I IFN]] is absolutely critical for resistance to viruses, there is growing literature about the negative role of [[type I interferon]] in host immunity mediated by STING. AT-rich stem-loop DNA motif in the ''[[Plasmodium falciparum]]'' and ''[[Plasmodium berghei]]'' genome and extracellular DNA from ''[[Mycobacterium tuberculosis]]'' have been shown to activate [[type I interferon]] through STING.<ref name="pmid21820332">{{cite journal | vauthors = Sharma S, DeOliveira RB, Kalantari P, Parroche P, Goutagny N, Jiang Z, Chan J, Bartholomeu DC, Lauw F, Hall JP, Barber GN, Gazzinelli RT, Fitzgerald KA, Golenbock DT | title = Innate immune recognition of an AT-rich stem-loop DNA motif in the Plasmodium falciparum genome | journal = Immunity | volume = 35 | issue = 2 | pages = 194–207 | date = Aug 2011 | pmid = 21820332 | pmc = 3162998 | doi = 10.1016/j.immuni.2011.05.016 }}</ref><ref name="pmid22607800">{{cite journal | vauthors = Manzanillo PS, Shiloh MU, Portnoy DA, Cox JS | title = Mycobacterium tuberculosis activates the DNA-dependent cytosolic surveillance pathway within macrophages | journal = Cell Host & Microbe | volume = 11 | issue = 5 | pages = 469–80 | date = May 2012 | pmid = 22607800 | doi = 10.1016/j.chom.2012.03.007 | pmc=3662372}}</ref> Perforation of the phagosome membrane mediated by [[ESX1]] secretion system allows extracellular mycobacterial DNA to access host cytosolic DNA sensors, thus inducing the production of [[type I interferon]] in macrophages. High [[type I interferon]] signature leads to the ''[[M. tuberculosis]]'' pathogenesis and prolonged infection.<ref name="pmid22607800" /> STING-TBK1-IRF mediated [[type I interferon]] response is central to the pathogenesis of experimental cerebral malaria in laboratory animals infected with ''[[Plasmodium berghei]]''. Laboratory mice deficient in [[type I interferon]] response are resistant to experimental cerebral malaria.<ref name="pmid21820332" />
== STING signaling mechanisms ==
[[File:STING signaling 20130422.png|thumb|420px|STING signaling]]
STING mediates [[Interferon type I|type I interferon]] immune response by functioning as both a direct DNA sensor and a [[Signal transducing adaptor protein|signaling adaptor protein]]. Upon activation, STING stimulates [[TANK-binding kinase 1|TBK1]] activity to [[Protein phosphorylation|phosphorylate]] [[IRF3]] or [[STAT6]]. Phosphorylated IRF3s and STAT6s dimerize, and then enter nucleus to stimulate expression of genes involved in host immune response, such as [[Interferon beta|IFNB]], [[CCL2]], [[CCL20]], etc.<ref name="pmid23238760" /><ref name="pmid22000020">{{cite journal | vauthors = Chen H, Sun H, You F, Sun W, Zhou X, Chen L, Yang J, Wang Y, Tang H, Guan Y, Xia W, Gu J, Ishikawa H, Gutman D, Barber G, Qin Z, Jiang Z | title = Activation of STAT6 by STING is critical for antiviral innate immunity | journal = Cell | volume = 147 | issue = 2 | pages = 436–46 | date = Oct 2011 | pmid = 22000020 | doi = 10.1016/j.cell.2011.09.022 | doi-access = free }}</ref>
Several reports suggested that STING is associated with the activation of selective autophagy.<ref name="pmid19926846" /> ''[[Mycobacterium tuberculosis]]'' has been shown to produce cytosolic DNA ligands which activate STING, resulting in [[ubiquitination]] of bacteria and the subsequent recruitment of [[autophagy]] related proteins, all of which are required for 'selective' autophagic targeting and innate defense against ''M. tuberculosis''.<ref name="pmid22901810">{{cite journal | vauthors = Watson RO, Manzanillo PS, Cox JS | title = Extracellular M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathway | journal = Cell | volume = 150 | issue = 4 | pages = 803–15 | date = Aug 2012 | pmid = 22901810 | pmc = 3708656 | doi = 10.1016/j.cell.2012.06.040 }}</ref>
In summary, STING coordinates multiple immune responses to infection, including the induction of interferons and STAT6-dependent response and selective autophagy response.<ref name="pmid23238760" />
=== As a cytosolic DNA sensor ===
[[Cyclic nucleotide|Cyclic dinucleotides]]-second-messenger signaling molecules produced by diverse bacterial species were detected in the cytosol of mammalian cells during intracellular pathogen infection; this leads to activation of [[TANK-binding kinase 1|TBK1]]-[[IRF3]] and the downstream production of [[Interferon type I|type I interferon]].<ref name="pmid23238760" /><ref name="pmid19652017">{{cite journal | vauthors = McWhirter SM, Barbalat R, Monroe KM, Fontana MF, Hyodo M, Joncker NT, Ishii KJ, Akira S, Colonna M, Chen ZJ, Fitzgerald KA, Hayakawa Y, Vance RE | title = A host type I interferon response is induced by cytosolic sensing of the bacterial second messenger cyclic-di-GMP | journal = The Journal of Experimental Medicine | volume = 206 | issue = 9 | pages = 1899–911 | date = Aug 2009 | pmid = 19652017 | pmc = 2737161 | doi = 10.1084/jem.20082874 | url = http://digitalcommons.wustl.edu/cgi/viewcontent.cgi?article=1539&context=open_access_pubs }}</ref>
STING has been shown to bind directly to [[cyclic di-GMP]], and this recognition leads to the production of [[cytokines]], such as [[Interferon type I|type I interferon]], that are essential for successful pathogen elimination.<ref name="pmid21947006">{{cite journal | vauthors = Burdette DL, Monroe KM, Sotelo-Troha K, Iwig JS, Eckert B, Hyodo M, Hayakawa Y, Vance RE | title = STING is a direct innate immune sensor of cyclic di-GMP | journal = Nature | volume = 478 | issue = 7370 | pages = 515–8 | date = Oct 2011 | pmid = 21947006 | pmc = 3203314 | doi = 10.1038/nature10429 | bibcode = 2011Natur.478..515B }}</ref>
=== As a signaling adaptor ===
[[DDX41]], a member of the DEXDc family of [[helicase]]s, in [[myeloid dendritic cell]]s recognizes intracellular DNA and mediates innate immune response through direct association with STING.<ref name="pmid21892174">{{cite journal | vauthors = Zhang Z, Yuan B, Bao M, Lu N, Kim T, Liu YJ | title = The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells | journal = Nature Immunology | volume = 12 | issue = 10 | pages = 959–65 | date = Oct 2011 | pmid = 21892174 | pmc = 3671854 | doi = 10.1038/ni.2091 }}</ref> Other DNA sensors- [[ZBP1|DAI]], [[RNA polymerase III]], [[IFI16]], have also been shown to activate STING through direct or indirect interactions.<ref name="pmid21940216" />
[[Cyclic GMP-AMP synthase]] (cGAS), which belongs to the [[nucleotidyltransferase]] family, is able to recognize cytosolic DNA contents and induce STING-dependent interferon response by producing secondary messenger [[cyclic guanosine monophosphate–adenosine monophosphate]] (cyclic GMP-AMP, or cGAMP). After [[cyclic guanosine monophosphate–adenosine monophosphate|cyclic GMP-AMP]] bound STING is activated, it enhances [[TANK-binding kinase 1|TBK1]]'s activity to phosphorylate [[IRF3]] and [[STAT6]] for downstream [[type I interferon]] response.<ref name="pmid23258412">{{cite journal | vauthors = Wu J, Sun L, Chen X, Du F, Shi H, Chen C, Chen ZJ | title = Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA | journal = Science | volume = 339 | issue = 6121 | pages = 826–30 | date = Feb 2013 | pmid = 23258412 | doi = 10.1126/science.1229963 | pmc=3855410| bibcode = 2013Sci...339..826W }}</ref><ref name="pmid23258413">{{cite journal | vauthors = Sun L, Wu J, Du F, Chen X, Chen ZJ | title = Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway | journal = Science | volume = 339 | issue = 6121 | pages = 786–91 | date = Feb 2013 | pmid = 23258413 | doi = 10.1126/science.1232458 | pmc=3863629| bibcode = 2013Sci...339..786S }}</ref>
It has been proposed that intracellular calcium plays an important role in the response of the STING pathway.<ref name="Calcium">{{cite bioRxiv | vauthors = Kim S, Koch P, Li L, Peshkin L, Mitchison TJ | title = Evidence for a role of calcium in STING signaling  | date = 4 Jun 2017 | biorxiv = 10.1101/145854  }}</ref>
== See also ==
* {{annotated link|STING agonist}}
== References ==
{{reflist|35em}}
== Further reading ==
{{refbegin | 2}}
* {{cite journal | vauthors = Wang Y, Tong X, Omoregie ES, Liu W, Meng S, Ye X | title = Tetraspanin 6 (TSPAN6) negatively regulates retinoic acid-inducible gene I-like receptor-mediated immune signaling in a ubiquitination-dependent manner | journal = The Journal of Biological Chemistry | volume = 287 | issue = 41 | pages = 34626–34 | date = Oct 2012 | pmid = 22908223 | pmc = 3464568 | doi = 10.1074/jbc.M112.390401 | doi-access = free }}
* {{cite journal | vauthors = Yin Q, Tian Y, Kabaleeswaran V, Jiang X, Tu D, Eck MJ, Chen ZJ, Wu H | title = Cyclic di-GMP sensing via the innate immune signaling protein STING | journal = Molecular Cell | volume = 46 | issue = 6 | pages = 735–45 | date = Jun 2012 | pmid = 22705373 | pmc = 3697849 | doi = 10.1016/j.molcel.2012.05.029 }}
* {{cite journal | vauthors = Aguirre S, Maestre AM, Pagni S, Patel JR, Savage T, Gutman D, Maringer K, Bernal-Rubio D, Shabman RS, Simon V, Rodriguez-Madoz JR, Mulder LC, Barber GN, Fernandez-Sesma A | title = DENV inhibits type I IFN production in infected cells by cleaving human STING | journal = PLOS Pathogens | volume = 8 | issue = 10 | pages = e1002934 | year = 2012 | pmid = 23055924 | pmc = 3464218 | doi = 10.1371/journal.ppat.1002934 | doi-access = free }}
* {{cite journal | vauthors = Li Y, Li C, Xue P, Zhong B, Mao AP, Ran Y, Chen H, Wang YY, Yang F, Shu HB | title = ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 19 | pages = 7945–50 | date = May 2009 | pmid = 19416887 | pmc = 2683125 | doi = 10.1073/pnas.0900818106 | bibcode = 2009PNAS..106.7945L | doi-access = free }}
* {{cite journal | vauthors = Conlon J, Burdette DL, Sharma S, Bhat N, Thompson M, Jiang Z, Rathinam VA, Monks B, Jin T, Xiao TS, Vogel SN, Vance RE, Fitzgerald KA | title = Mouse, but not human STING, binds and signals in response to the vascular disrupting agent 5,6-dimethylxanthenone-4-acetic acid | journal = Journal of Immunology | volume = 190 | issue = 10 | pages = 5216–25 | date = May 2013 | pmid = 23585680 | pmc = 3647383 | doi = 10.4049/jimmunol.1300097 }}
* {{cite journal | vauthors = Abe T, Harashima A, Xia T, Konno H, Konno K, Morales A, Ahn J, Gutman D, Barber GN | title = STING recognition of cytoplasmic DNA instigates cellular defense | journal = Molecular Cell | volume = 50 | issue = 1 | pages = 5–15 | date = Apr 2013 | pmid = 23478444 | pmc = 3881179 | doi = 10.1016/j.molcel.2013.01.039 }}
* {{cite journal | vauthors = Nazmi A, Mukhopadhyay R, Dutta K, Basu A | title = STING mediates neuronal innate immune response following Japanese encephalitis virus infection | journal = Scientific Reports | volume = 2 | pages = 347 | year = 2012 | pmid = 22470840 | pmc = 3317237 | doi = 10.1038/srep00347 | bibcode = 2012NatSR...2E.347N }}
* {{cite journal | vauthors = Zhang J, Hu MM, Wang YY, Shu HB | title = TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/STING protein for K63-linked ubiquitination | journal = The Journal of Biological Chemistry | volume = 287 | issue = 34 | pages = 28646–55 | date = Aug 2012 | pmid = 22745133 | pmc = 3436586 | doi = 10.1074/jbc.M112.362608 | doi-access = free }}
* {{cite journal | vauthors = Ishikawa H, Barber GN | title = STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling | journal = Nature | volume = 455 | issue = 7213 | pages = 674–8 | date = Oct 2008 | pmid = 18724357 | pmc = 2804933 | doi = 10.1038/nature07317 | bibcode = 2008Natur.455..674I }}
{{refend}}
{{Pattern recognition receptors}}
{{Adaptor proteins}}
[[Category:Immune system]]
[[Category:Intracellular receptors]]