ER-localized JmjC domain-containing protein JMJD8 targets STING to promote immune evasion and tumor growth in breast cancer

Sung "Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries" CA Cancer J. Clin. (2021)

[2]

Wu "Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA" Science (2013) 10.1126/science.1229963

[3]

Sun "Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the Type I interferon pathway" Science (2013) 10.1126/science.1232458

[4]

Li "Cyclic GMP-AMP synthase is activated by double-stranded DNA-induced oligomerization" Immunity (2013) 10.1016/j.immuni.2013.10.019

[5]

Zhang "The cytosolic DNA sensor cGAS forms an oligomeric complex with DNA and undergoes switch-like conformational changes in the activation loop" Cell Rep. (2014) 10.1016/j.celrep.2014.01.003

[6]

Ablasser "Cell intrinsic immunity spreads to bystander cells via the intercellular transfer of cGAMP" Nature (2013) 10.1038/nature12640

[7]

Civril "Structural mechanism of cytosolic DNA sensing by cGAS" Nature (2013) 10.1038/nature12305

[8]

Diner "The innate immune DNA sensor cGAS produces a noncanonical cyclic dinucleotide that activates human STING" Cell Rep. (2013) 10.1016/j.celrep.2013.05.009

[9]

Gao "Cyclic [G(2 ′,5 ′) pA(3 ′,5 ′)p] Is the Metazoan Second Messenger" Cell (2013) 10.1016/j.cell.2013.04.046

[10]

Gao "Structure-Function Analysis of STING Activation by c[G(2 ′,5 ′) pA(3 ′,5 ′)p] and Targeting by antiviral DMXAA" Cell (2013) 10.1016/j.cell.2013.07.023

[11]

STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity

Hiroki Ishikawa, Zhe Ma, Glen N. Barber

Nature 2009 10.1038/nature08476

[12]

Saitoh "Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response" Proc. Natl. Acad. Sci. USA (2009) 10.1073/pnas.0911267106

[13]

Sharma "Triggering the interferon antiviral response through an IKK-related pathway" Science (2003) 10.1126/science.1081315

[14]

Tanaka "STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway" Sci. Signal. (2012) 10.1126/scisignal.2002521

[15]

Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation

Siqi Liu, Xin Cai, Jianguo Wu et al.

Science 2015 10.1126/science.aaa2630

[16]

Ishikawa "The STING pathway and regulation of innate immune signaling in response to DNA pathogens" Cell. Mol. Life Sci. (2011) 10.1007/s00018-010-0605-2

[17]

Corrales "Direct activation of STING in the tumor microenvironment leads to potent and systemic tumor regression and immunity" Cell Rep. (2015) 10.1016/j.celrep.2015.04.031

[18]

Demaria "STING activation of tumor endothelial cells initiates spontaneous and therapeutic antitumor immunity" Proc. Natl. Acad. Sci. USA (2015) 10.1073/pnas.1512832112

[19]

Curran "STING pathway activation stimulates potent immunity against acute myeloid leukemia" Cell Rep. (2016) 10.1016/j.celrep.2016.05.023

[20]

Yum "Roles of the cGAS-STING pathway in cancer immunosurveillance and immunotherapy" Annu. Rev. Canc. Biol. (2019) 10.1146/annurev-cancerbio-030518-055636

[21]

Driessens "Assessment of in vivo chemotherapy-induced DNA damage in a p53-mutated rat tumor by micronuclei assay: from signaling pathways to therapeutic tools" Ann. N. Y. Acad. Sci. (2003) 10.1196/annals.1299.139

[22]

Radiation-Induced Chromosomal Aberrations and Immunotherapy: Micronuclei, Cytosolic DNA, and Interferon-Production Pathway

Marco Durante, Silvia C. Formenti

Frontiers in Oncology 2018 10.3389/fonc.2018.00192

[23]

Dou "Cytoplasmic chromatin triggers inflammation in senescence and cancer" Nature (2017) 10.1038/nature24050

[24]

Bu "Decreased expression of TMEM173 predicts poor prognosis in patients with hepatocellular carcinoma" PLoS One (2016) 10.1371/journal.pone.0165681

[25]

Song "Decreased expression of STING predicts poor prognosis in patients with gastric cancer" Sci. Rep.-Uk (2017)

[26]

Ahn "Diverse roles of STING-dependent signaling on the development of cancer" Oncogene (2015) 10.1038/onc.2014.457

[27]

Tsukada "Histone demethylation by a family of JmjC domain-containing proteins" Nature (2006) 10.1038/nature04433

[28]

Klose "JmjC-domain-containing proteins and histone demethylation" Nat. Rev. Genet. (2006) 10.1038/nrg1945

[29]

Lando "FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor" Genes Dev. (2002) 10.1101/gad.991402

[30]

Trewick "Methylation: lost in hydroxylation?" EMBO Rep. (2005) 10.1038/sj.embor.7400379

[31]

Webby "Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing" Science (2009) 10.1126/science.1175865

[32]

Ploumakis "OH, the places You'll Go! hydroxylation, gene expression, and cancer" Mol. Cell (2015) 10.1016/j.molcel.2015.05.026

[33]

Oh "The small members of the JMJD protein family: enzymatic jewels or jinxes?" Biochim. Biophys. Acta Rev. Cancer (2019) 10.1016/j.bbcan.2019.04.002

[34]

Wilkins "JMJD5 is a human arginyl C-3 hydroxylase" Nat. Commun. (2018)

[35]

Koyama-Nasu "The F-box protein Fbl10 is a novel transcriptional repressor of c-Jun" Nat. Cell Biol. (2007) 10.1038/ncb1628

[36]

Yi "JMJD6 and U2AF65 co-regulate alternative splicing in both JMJD6 enzymatic activity dependent and independent manner" Nucleic Acids Res. (2017) 10.1093/nar/gkw1144

[37]

Pedersen "Histone demethylases in development and disease" Trends Cell Biol. (2010) 10.1016/j.tcb.2010.08.011

[38]

Suzuki "Identification of Myc-associated protein with JmjC domain as a novel therapeutic target oncogene for lung cancer" Mol. Cancer Ther. (2007) 10.1158/1535-7163.mct-06-0659

[39]

Kooistra "Molecular mechanisms and potential functions of histone demethylases" Nat. Rev. Mol. Cell Biol. (2012) 10.1038/nrm3327

[40]

Tran "Lysine demethylase KDM6A in differentiation, development, and cancer" Mol. Cell. Biol. (2020) 10.1128/mcb.00341-20

[41]

Herr "Amazing diversity in biochemical roles of Fe(II)/2-oxoglutarate oxygenases" Trends Biochem. Sci. (2018) 10.1016/j.tibs.2018.04.002

[42]

Loenarz "Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases" Trends Biochem. Sci. (2011) 10.1016/j.tibs.2010.07.002

[43]

Shi "Histone lysine demethylases: emerging roles in development, physiology and disease" Nat. Rev. Genet. (2007) 10.1038/nrg2218

[44]

Wu "KDM5 histone demethylases repress immune response via suppression of STING" PLoS Biol. (2018) 10.1371/journal.pbio.2006134

[45]

Shen "The dual function of KDM5C in both gene transcriptional activation and repression promotes breast cancer cell growth and tumorigenesis" Adv. Sci. (Weinh) (2021)

[46]

Zhang "KDM5B promotes immune evasion by recruiting SETDB1 to silence retroelements" Nature (2021) 10.1038/s41586-021-03994-2

[47]

Chen "Methyltransferase SETD2-mediated methylation of STAT1 is critical for interferon antiviral activity" Cell (2017) 10.1016/j.cell.2017.06.042

[48]

Zhang "The methyltransferase PRMT6 attenuates antiviral innate immunity by blocking TBK1-IRF3 signaling" Cell. Mol. Immunol. (2019) 10.1038/s41423-018-0057-4

[49]

Su "JmjC domain-containing protein 8 (JMJD8) represses Ku70/Ku80 expression via attenuating AKT/NF-kappa B/COX-2 signaling" Biochim. Biophys. Acta Mol. Cell Res. (2019) 10.1016/j.bbamcr.2019.118541

[50]

Wang "MiR-873-5p suppresses cell proliferation and epithelial-mesenchymal transition via directly targeting Jumonji domain-containing protein 8 through the NF-kappa B pathway in colorectal cancer" J. Cell Commun. Signal. (2019) 10.1007/s12079-019-00522-w

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ER: a critical hub for STING signaling regulation

Yuan Luo, Lei Chang · 2024

Trends in Cell Biology

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Details

Published: May 01, 2023
Vol/Issue: 58(9)
Pages: 760-778.e6
License: View

Authors

The Jack H. Skirball Center for Chemical Biology & Proteomics, The Salk Institute for Biological Studies, La Jolla, California 92037

School of Chemical Engineering, The University of Adelaide, Adelaide, SA 5005, Australia.

National Lab of Pattern Recognition, Institute of Automation, Chinese Academy of Sciences

G

Guosheng Hu

Biomedical Research Center of South China, College of Life Sciences, Fujian Normal University

Department of Clinical Oncology, Institute of Development, Aging, and Cancer, Tohoku University, Sendai 980-8575, Japan

Funding

National Natural Science Foundation of China Award: 31871319

Fundamental Research Funds for the Central Universities Award: 20720190145

China Postdoctoral Science Foundation Award: 2020M682097

Natural Science Foundation of Fujian Province Award: 2020J02004

National Key Research and Development Program of China Award: 2020YFA0112300

Cite This Article

Jia Yi, Lei Wang, Jiao Du, et al. (2023). ER-localized JmjC domain-containing protein JMJD8 targets STING to promote immune evasion and tumor growth in breast cancer. Developmental Cell, 58(9), 760-778.e6. https://doi.org/10.1016/j.devcel.2023.03.015

ER-localized JmjC domain-containing protein JMJD8 targets STING to promote immune evasion and tumor growth in breast cancer

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