The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Activation of STING requires palmitoylation at the Golgi
Open accessAbstract
Stimulator of interferon genes (STING) is essential for the type I interferon response against DNA pathogens. In response to the presence of DNA and/or cyclic dinucleotides, STING translocates from the endoplasmic reticulum to perinuclear compartments. However, the role of this subcellular translocation remains poorly defined. Here we show that palmitoylation of STING at the Golgi is essential for activation of STING. Treatment with palmitoylation inhibitor 2-bromopalmitate (2-BP) suppresses palmitoylation of STING and abolishes the type I interferon response. Mutation of two membrane-proximal Cys residues (Cys88/91) suppresses palmitoylation, and this STING mutant cannot induce STING-dependent host defense genes. STING variants that constitutively induce the type I interferon response were found in patients with autoimmune diseases. The response elicited by these STING variants is effectively inhibited by 2-BP or an introduction of Cys88/91Ser mutation. Our results may lead to new treatments for cytosolic DNA-triggered autoinflammatory diseases.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Pattern Recognition Receptors and Inflammation
Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895
Yoneyama, M., Kikuchi, M., Natsukawa, T., Shinobu, N., Imaizumi, T., Miyagishi, M., Taira, K., Akira, S., & Fujita, T. (2004) · Nature Immunology · doi:10.1038/ni1087 · Cited by 3,929
STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
Ishikawa, H., & Barber, G. N. (2008) · Nature · doi:10.1038/nature07317 · Cited by 3,576
Self-citationSTING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
Ishikawa, H., Ma, Z., & Barber, G. N. (2009) · Nature · doi:10.1038/nature08476 · Cited by 2,759 · cited 6×
“The C88/91S mutant was used to determine whether palmitoylation is also needed in the host defense response against DNA viruses 6 .”
InfluentialSelf-citationCyclic GMP-AMP Is an Endogenous Second Messenger in Innate Immune Signaling by Cytosolic DNA
Wu, J., Sun, L., Chen, X., Du, F., Shi, H., Chen, C., & Chen, Z. J. (2013) · Science · doi:10.1126/science.1229963 · Cited by 2,541
Mitochondrial DNA stress primes the antiviral innate immune response
West, A. P., Khoury-Hanold, W., Staron, M., Tal, M. C., Pineda, C. M., Lang, S. M., Bestwick, M., Duguay, B. A., Raimundo, N., MacDuff, D. A., et al. (2015) · Nature · doi:10.1038/nature14156 · Cited by 1,975
STING is a direct innate immune sensor of cyclic di-GMP
Burdette, D. L., Monroe, K. M., Sotelo-Troha, K., Iwig, J. S., Eckert, B., Hyodo, M., Hayakawa, Y., & Vance, R. E. (2011) · Nature · doi:10.1038/nature10429 · Cited by 1,570
The Adaptor Protein MITA Links Virus-Sensing Receptors to IRF3 Transcription Factor Activation
Zhong, B., Yang, Y., Li, S., Wang, Y.-Y., Li, Y., Diao, F., Lei, C., He, X., Zhang, L., Tien, P., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.09.003 · Cited by 1,519
Activated STING in a Vascular and Pulmonary Syndrome
Liu, Y., Jesus, A. A., Marrero, B., Yang, D., Ramsey, S. E., Montealegre Sanchez, G. A., Tenbrock, K., Wittkowski, H., Jones, O. Y., Kuehn, H. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1312625 · Cited by 1,412
Intracellular Toll-like Receptors
Blasius, A. L., & Beutler, B. (2010) · Immunity · doi:10.1016/j.immuni.2010.03.012 · Cited by 1,325
STING Specifies IRF3 Phosphorylation by TBK1 in the Cytosolic DNA Signaling Pathway
Tanaka, Y., & Chen, Z. J. (2012) · Science Signaling · doi:10.1126/scisignal.2002521 · Cited by 1,317
Palmitoylation: policing protein stability and traffic
Linder, M. E., & Deschenes, R. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2084 · Cited by 1,185
The trans Golgi Network: Sorting at the Exit Site of the Golgi Complex
Griffiths, G., & Simons, K. (1986) · Science · doi:10.1126/science.2945253 · Cited by 1,185
Recognition of Cytosolic DNA Activates an IRF3-Dependent Innate Immune Response
Stetson, D. B., & Medzhitov, R. (2006) · Immunity · doi:10.1016/j.immuni.2005.12.003 · Cited by 1,008
Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H.-P., Yuan, L. C., & Klausner, R. D. (1990) · Cell · doi:10.1016/0092-8674(90)90096-w · Cited by 967
Sun, W., Li, Y., Chen, L., Chen, H., You, F., Zhou, X., Zhou, Y., Zhai, Z., Chen, D., & Jiang, Z. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900850106 · Cited by 866
Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response
Saitoh, T., Fujita, N., Hayashi, T., Takahara, K., Satoh, T., Lee, H., Matsunaga, K., Kageyama, S., Omori, H., Noda, T., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911267106 · Cited by 854
Woodward, J. J., Iavarone, A. T., & Portnoy, D. A. (2010) · Science · doi:10.1126/science.1189801 · Cited by 810
Lee-Kirsch, M. A., Gong, M., Chowdhury, D., Senenko, L., Engel, K., Lee, Y.-A., de Silva, U., Bailey, S. L., Witte, T., Vyse, T. J., et al. (2007) · Nature Genetics · doi:10.1038/ng2091 · Cited by 730 · cited 4×
“Mice lacking DNase II or DNase III (Trex1) die during embryonic development or within 10 weeks of birth, respectively, with inflammation-related phenotypes.”
InfluentialPattern recognition receptors and control of adaptive immunity
Palm, N. W., & Medzhitov, R. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00731.x · Cited by 729
Konno, H., Konno, K., & Barber, G. N. (2013) · Cell · doi:10.1016/j.cell.2013.09.049 · Cited by 687
Self-citationDobbs, N., Burnaevskiy, N., Chen, D., Gonugunta, V. K., Alto, N. M., & Yan, N. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.07.001 · Cited by 630
Jeremiah, N., Neven, B., Gentili, M., Callebaut, I., Maschalidi, S., Stolzenberg, M.-C., Goudin, N., Frémond, M.-L., Nitschke, P., Molina, T. J., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci79100 · Cited by 562
Identification of PSD-95 Palmitoylating Enzymes
Fukata, M., Fukata, Y., Adesnik, H., Nicoll, R. A., & Bredt, D. S. (2004) · Neuron · doi:10.1016/j.neuron.2004.12.005 · Cited by 533
Gall, A., Treuting, P., Elkon, K. B., Loo, Y.-M., Gale, M., Barber, G. N., & Stetson, D. B. (2012) · Immunity · doi:10.1016/j.immuni.2011.11.018 · Cited by 510
Self-citationSTING manifests self DNA-dependent inflammatory disease
Ahn, J., Gutman, D., Saijo, S., & Barber, G. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215006109 · Cited by 509
Self-citationDe Matteis, M. A., & Luini, A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2378 · Cited by 483
Jin, L., Waterman, P. M., Jonscher, K. R., Short, C. M., Reisdorph, N. A., & Cambier, J. C. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00640-08 · Cited by 450
Rice, G., Newman, W. G., Dean, J., Patrick, T., Parmar, R., Flintoff, K., Robins, P., Harvey, S., Hollis, T., O’Hara, A., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/513443 · Cited by 410
Ouyang, S., Song, X., Wang, Y., Ru, H., Shaw, N., Jiang, Y., Niu, F., Zhu, Y., Qiu, W., Parvatiyar, K., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.03.019 · Cited by 350
Soulat, D., Bürckstümmer, T., Westermayer, S., Goncalves, A., Bauch, A., Stefanovic, A., Hantschel, O., Bennett, K. L., Decker, T., & Superti-Furga, G. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.126 · Cited by 325
STING Recognition of Cytoplasmic DNA Instigates Cellular Defense
Abe, T., Harashima, A., Xia, T., Konno, H., Konno, K., Morales, A., Ahn, J., Gutman, D., & Barber, G. N. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.039 · Cited by 299
Self-citationPartitioning of the Golgi Apparatus during Mitosis in Living HeLa Cells
Shima, D. T., Haldar, K., Pepperkok, R., Watson, R., & Warren, G. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.6.1211 · Cited by 222
NLR, the nucleotide-binding domain leucine-rich repeat containing gene family
Ye, Z., & Ting, J. P.-Y. (2008) · Current Opinion in Immunology · doi:10.1016/j.coi.2008.01.003 · Cited by 219
Intrinsic Self-DNA Triggers Inflammatory Disease Dependent on STING
Ahn, J., Ruiz, P., & Barber, G. N. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401337 · Cited by 184
Self-citationSelf-DNA, STING-dependent signaling and the origins of autoinflammatory disease
Ahn, J., & Barber, G. N. (2014) · Current Opinion in Immunology · doi:10.1016/j.coi.2014.10.009 · Cited by 142
Self-citationUemura, T., Yamamoto, M., Kametaka, A., Sou, Y., Yabashi, A., Yamada, A., Annoh, H., Kametaka, S., Komatsu, M., & Waguri, S. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01327-13 · Cited by 141
Self-citationAssays of protein palmitoylation
Drisdel, R. C., Alexander, J. K., Sayeed, A., et al. (2006) · Methods · doi:10.1016/j.ymeth.2006.04.015 · Cited by 132
Sphingomyelin organization is required for vesicle biogenesis at the Golgi complex
Durán, J. M., Campelo, F., van Galen, J., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.317 · Cited by 101
Spatial segregation of degradation- and recycling-trafficking pathways in COS-1 cells
Misaki, R., Nakagawa, T., Fukuda, M., Taniguchi, N., & Taguchi, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.101 · Cited by 39
Self-citation
Cited by
Regulation and function of the cGAS–STING pathway of cytosolic DNA sensing
Chen, Q., Sun, L., & Chen, Z. J. (2016) · Nature Immunology · doi:10.1038/ni.3558 · Cited by 2,333
The cGAS–STING pathway as a therapeutic target in inflammatory diseases
Decout, A., Katz, J. D., Venkatraman, S., & Ablasser, A. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00524-z · Cited by 2,309
Molecular mechanisms and cellular functions of cGAS–STING signalling
Hopfner, K.-P., & Hornung, V. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0244-x · Cited by 2,052
Role of neuroinflammation in neurodegeneration development
Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668
“cGAMP produced by cGAS activation binds to STING which is located on the membrane of endoplasmic reticulum (ER)(391) and leads to the translocation of STING from ER to the Golgi where it is further modified.(392) On reaching the Golgi compartment, STING then recruits TBK1, which then activates IRF3 and NF-κB, leading…”
BackgroundDNA sensing by the cGAS–STING pathway in health and disease
Motwani, M., Pesiridis, S., & Fitzgerald, K. A. (2019) · Nature Reviews Genetics · doi:10.1038/s41576-019-0151-1 · Cited by 1,467
Metadata
- Authors
- Mukai, K., Konno, H., Akiba, T., Uemura, T., Waguri, S., Kobayashi, T., Barber, G. N., Arai, H., & Taguchi, T.
- Venue
- Nature Communications
- Published
- 2016-06-21
- Volume
- 7
- Issue
- 1
- Pages
- 11932-11932
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2469317767
- Cited by
- 710
- References
- 40
- FWCI
- 12.79
- Type
- journal article
- Language
- en
- Open access
- gold
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
