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.
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Cites
Pattern Recognition Receptors and Inflammation
Takeuchi, O., & Akira, S. (2010) · Cell · doi:10.1016/j.cell.2010.01.022 · Cited by 8,895
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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
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
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- Mukai, K., Konno, H., Akiba, T., Uemura, T., Waguri, S., Kobayashi, T., Barber, G. N., Arai, H., & Taguchi, T. (2016). Activation of STING requires palmitoylation at the Golgi. Nature Communications. https://doi.org/10.1038/ncomms11932
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