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FBXW7 is a multifaceted regulator of the innate immune response to DNA viruses

Cellular & Molecular Immunology volume 22, pages 1427–1443 (2025) Cite this article

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Abstract

Upon DNA virus infection, cGAS senses viral DNA and triggers MITA (also called STING)-dependent induction of type I interferons (IFN-Is) and other cytokines/chemokines. IFN-Is further activate STAT1/2 to induce interferon-stimulated genes (ISGs) and the innate antiviral response. How the innate antiviral response is silenced in uninfected cells and efficiently mounts upon viral infection is not fully understood. In this study, we found that FBXW7, a substrate recognition component of the SCF E3 ubiquitin ligase complex, is a multifaceted regulator of the innate immune response to DNA viruses. In uninfected cells, FBXW7 mediates the polyubiquitination and degradation of GSK3α/β-phosphorylated SLC35B2/3 at the Golgi apparatus. This leads to the downregulation of sulfated glycosaminoglycans (sGAGs) in the Golgi apparatus and the inactivation of MITA in uninfected cells. In addition, FBXW7 mediates the degradation of GSK3α/β-phosphorylated MYC, which is a repressor of STAT1/2, leading to proper STAT1/2 levels in uninfected cells. The differential regulation of FBXW7 on MITA and STAT1/2 ensures inactivation but is ready for fast mount of the innate immune response in uninfected cells. Infection with DNA viruses activates the PI3K‒AKT axis, which inactivates GSK3α/β and inhibits FBXW7-mediated polyubiquitination and degradation of SLC35B2/3, leading to increased production of sGAGs, activation of MITA and rapid onset of the innate antiviral response. Consistently, gene disruption experiments indicate that FBXW7 modulates the innate antiviral response in human THP-1 and mouse BMDM cells. These findings suggest that FBXW7 functions as a versatile regulator of the innate immune response to DNA viruses by differentially regulating upstream and downstream components of the type I interferon induction loop.

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References

  1. Sun L, Wu J, Du F, Chen X, Chen ZJ. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science. 2013;339:786–91. https://doi.org/10.1126/science.1232458.

    Article  PubMed  CAS  Google Scholar 

  2. Ablasser A, Goldeck M, Cavlar T, Deimling T, Witte G, Röhl I, et al. cGAS produces a 2’-5’-linked cyclic dinucleotide second messenger that activates STING. Nature. 2013;498:380–4. https://doi.org/10.1038/nature12306.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  3. Luo WW, Shu HB. Delicate regulation of the cGAS-MITA-mediated innate immune response. Cell Mol Immunol. 2018;15:666–75. https://doi.org/10.1038/cmi.2016.51.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  4. Zhong B, Yang Y, Li S, Wang YY, Li Y, Diao F, et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity. 2008;29:538–50. https://doi.org/10.1016/j.immuni.2008.09.003.

    Article  PubMed  CAS  Google Scholar 

  5. Dobbs N, Burnaevskiy N, Chen D, Gonugunta VK, Alto NM, Yan N. STING activation by translocation from the ER Is associated with infection and autoinflammatory disease. Cell Host Microbe. 2015;18:157–68. https://doi.org/10.1016/j.chom.2015.07.001.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  6. Fang R, Jiang Q, Guan Y, Gao P, Zhang R, Zhao Z, et al. Golgi apparatus-synthesized sulfated glycosaminoglycans mediate polymerization and activation of the cGAMP sensor STING. Immunity. 2021;54:962–.e968. https://doi.org/10.1016/j.immuni.2021.03.011.

    Article  PubMed  CAS  Google Scholar 

  7. Hu MM, Shu HB. Cytoplasmic mechanisms of recognition and defense of microbial nucleic acids. Annu Rev Cell Dev Biol. 2018;34:357–79. https://doi.org/10.1146/annurev-cellbio-100617-062903.

    Article  PubMed  CAS  Google Scholar 

  8. Hopfner KP, Hornung V. Molecular mechanisms and cellular functions of cGAS-STING signaling. Nat Rev Mol Cell Biol. 2020;21:501–21. https://doi.org/10.1038/s41580-020-0244-x.

    Article  PubMed  CAS  Google Scholar 

  9. Schoggins JW, Wilson SJ, Panis M, Murphy MY, Jones CT, Bieniasz P, et al. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature. 2011;472:481–5. https://doi.org/10.1038/nature09907.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  10. Chawla-Sarkar M, Lindner DJ, Liu YF, Williams BR, Sen GC, Silverman RH, et al. Apoptosis and interferons: role of interferon-stimulated genes as mediators of apoptosis. Apoptosis. 2003;8:237–49. https://doi.org/10.1023/a:1023668705040.

    Article  PubMed  CAS  Google Scholar 

  11. Lam KC, Araya RE, Huang A, Chen Q, Di Modica M, Rodrigues RR, et al. Microbiota triggers STING-type I IFN-dependent monocyte reprogramming of the tumor microenvironment. Cell. 2021;184:5338–56.e5321. https://doi.org/10.1016/j.cell.2021.09.019.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  12. Brenner E, Schörg BF, Ahmetlić F, Wieder T, Hilke FJ, Simon N, et al. Cancer immune control needs senescence induction by interferon-dependent cell cycle regulator pathways in tumors. Nat Commun. 2020;11:1335. https://doi.org/10.1038/s41467-020-14987-6.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  13. Chou WC, Rampanelli E, Li X, Ting JP. Impact of intracellular innate immune receptors on immunometabolism. Cell Mol Immunol. 2022;19:337–51. https://doi.org/10.1038/s41423-021-00780-y.

    Article  PubMed  CAS  Google Scholar 

  14. Hu MM, Shu HB. Mitochondrial DNA-triggered innate immune response: mechanisms and diseases. Cell Mol Immunol. 2023;20:1403–12. https://doi.org/10.1038/s41423-023-01086-x.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  15. Decout A, Katz JD, Venkatraman S, Ablasser A. The cGAS-STING pathway as a therapeutic target in inflammatory diseases. Nat Rev Immunol. 2021;21:548–69. https://doi.org/10.1038/s41577-021-00524-z.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  16. Zhang X, Bai XC, Chen ZJ. Structures and mechanisms in the cGAS-STING Innate Immunity Pathway. Immunity. 2020;53:43–53. https://doi.org/10.1016/j.immuni.2020.05.013.

    Article  PubMed  CAS  Google Scholar 

  17. Dai J, Huang YJ, He X, Zhao M, Wang X, Liu ZS, et al. Acetylation Blocks cGAS Activity and Inhibits Self-DNA-Induced Autoimmunity. Cell. 2019;176:1447–60.e1414. https://doi.org/10.1016/j.cell.2019.01.016.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  18. Hansen AL, Mukai K, Schopfer FJ, Taguchi T, Holm CK. STING palmitoylation as a therapeutic target. Cell Mol Immunol. 2019;16:236–41. https://doi.org/10.1038/s41423-019-0205-5.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  19. Kato Y, Park J, Takamatsu H, Konaka H, Aoki W, Aburaya S, et al. Apoptosis-derived membrane vesicles drive the cGAS-STING pathway and enhance type I IFN production in systemic lupus erythematosus. Ann Rheum Dis. 2018;77:1507–15. https://doi.org/10.1136/annrheumdis-2018-212988.

    Article  PubMed  CAS  Google Scholar 

  20. Liu Y, Jesus AA, Marrero B, Yang D, Ramsey SE, Sanchez GAM, et al. Activated STING in a vascular and pulmonary syndrome. N Engl J Med. 2014;371:507–18. https://doi.org/10.1056/NEJMoa1312625.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  21. Barnett KC, Coronas-Serna JM, Zhou W, Ernandes MJ, Cao A, Kranzusch PJ, et al. Phosphoinositide interactions position cGAS at the plasma membrane to ensure efficient distinction between self- and viral DNA. Cell. 2019;176:1432–46.e1411. https://doi.org/10.1016/j.cell.2019.01.049.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  22. Xia P, Ye B, Wang S, Zhu X, Du Y, Xiong Z, et al. Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity. Nat Immunol. 2016;17:369–78. https://doi.org/10.1038/ni.3356.

    Article  PubMed  CAS  Google Scholar 

  23. Zhong L, Hu MM, Bian LJ, Liu Y, Chen Q, Shu HB. Phosphorylation of cGAS by CDK1 impairs self-DNA sensing in mitosis. Cell Discov. 2020;6:26 https://doi.org/10.1038/s41421-020-0162-2.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  24. Welcker M, Orian A, Jin J, Grim JE, Harper JW, Eisenman RN, et al. The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc Natl Acad Sci USA. 2004;101:9085–90. https://doi.org/10.1073/pnas.0402770101.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  25. Strohmaier H, Spruck CH, Kaiser P, Won KA, Sangfelt O, Reed SI. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature. 2001;413:316–22. https://doi.org/10.1038/35095076.

    Article  PubMed  CAS  Google Scholar 

  26. Nateri AS, Riera-Sans L, Da Costa C, Behrens A. The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling. Science. 2004;303:1374–8. https://doi.org/10.1126/science.1092880.

    Article  PubMed  CAS  Google Scholar 

  27. Yada M, Hatakeyama S, Kamura T, Nishiyama M, Tsunematsu R, Imaki H, et al. Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. Embo J. 2004;23:2116–25. https://doi.org/10.1038/sj.emboj.7600217.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  28. Popov N, Wanzel M, Madiredjo M, Zhang D, Beijersbergen R, Bernards R, et al. The ubiquitin-specific protease USP28 is required for MYC stability. Nat Cell Biol. 2007;9:765–74. https://doi.org/10.1038/ncb1601.

    Article  PubMed  CAS  Google Scholar 

  29. Tsunematsu R, Nakayama K, Oike Y, Nishiyama M, Ishida N, Hatakeyama S, et al. Mouse Fbw7/Sel-10/Cdc4 is required for notch degradation during vascular development. J Biol Chem. 2004;279:9417–23. https://doi.org/10.1074/jbc.M312337200.

    Article  PubMed  CAS  Google Scholar 

  30. Inuzuka H, Shaik S, Onoyama I, Gao D, Tseng A, Maser RS, et al. SCF(FBW7) regulates apoptosis by targeting MCL1 for ubiquitylation and destruction. Nature. 2011;471:104–9. https://doi.org/10.1038/nature09732.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  31. Busino L, Millman SE, Scotto L, Kyratsous CA, Basrur V, O’Connor O, et al. Fbxw7α- and GSK3-mediated degradation of p100 is a pro-survival mechanism in multiple myeloma. Nat Cell Biol. 2012;14:375–85. https://doi.org/10.1038/ncb2463.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  32. Kumadaki S, Karasawa T, Matsuzaka T, Ema M, Nakagawa Y, Nakakuki M, et al. Inhibition of ubiquitin ligase F-box and WD repeat domain-containing 7α (Fbw7α) causes hepatosteatosis through Krüppel-like factor 5 (KLF5)/peroxisome proliferator-activated receptor γ2 (PPARγ2) pathway but not SREBP-1c protein in mice. J Biol Chem. 2011;286:40835–46. https://doi.org/10.1074/jbc.M111.235283.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  33. Davis RJ, Welcker M, Clurman BE. Tumor suppression by the Fbw7 ubiquitin ligase: mechanisms and opportunities. Cancer Cell. 2014;26:455–64. https://doi.org/10.1016/j.ccell.2014.09.013.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  34. Song Y, Lai L, Chong Z, He J, Zhang Y, Xue Y, et al. E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses. Nat Commun. 2017;8:14654. https://doi.org/10.1038/ncomms14654.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  35. Darnell JE Jr, Kerr IM, Stark GR. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science. 1994;264:1415–21. https://doi.org/10.1126/science.8197455.

    Article  PubMed  CAS  Google Scholar 

  36. Hu MM, Shu HB. Innate immune response to Cytoplasmic DNA: mechanisms and diseases. Annu Rev Immunol. 2020;38:79–98. https://doi.org/10.1146/annurev-immunol-070119-115052.

    Article  PubMed  CAS  Google Scholar 

  37. Cai X, Chiu YH, Chen ZJ. The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling. Mol Cell. 2014;54:289–96. https://doi.org/10.1016/j.molcel.2014.03.040.

    Article  PubMed  CAS  Google Scholar 

  38. Schneider WM, Chevillotte MD, Rice CM. Interferon-stimulated genes: a complex web of host defenses. Annu Rev Immunol. 2014;32:513–45. https://doi.org/10.1146/annurev-immunol-032713-120231.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  39. Grandvaux N, Servant MJ, tenOever B, Sen GC, Balachandran S, Barber GN, et al. Transcriptional profiling of interferon regulatory factor 3 target genes: direct involvement in the regulation of interferon-stimulated genes. J Virol. 2002;76:5532–9. https://doi.org/10.1128/jvi.76.11.5532-5539.2002.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  40. Hao B, Oehlmann S, Sowa ME, Harper JW, Pavletich NP. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol Cell. 2007;26:131–43. https://doi.org/10.1016/j.molcel.2007.02.022.

    Article  PubMed  CAS  Google Scholar 

  41. Duda DM, Olszewski JL, Tron AE, Hammel M, Lambert LJ, Waddell MB, et al. Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. Mol Cell. 2012;47:371–82. https://doi.org/10.1016/j.molcel.2012.05.044.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  42. Bai C, Sen P, Hofmann K, Ma L, Goebl M, Harper JW, et al. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell. 1996;86:263–74. https://doi.org/10.1016/s0092-8674(00)80098-7.

    Article  PubMed  CAS  Google Scholar 

  43. Nash P, Tang X, Orlicky S, Chen Q, Gertler FB, Mendenhall MD, et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature. 2001;414:514–21. https://doi.org/10.1038/35107009.

    Article  PubMed  CAS  Google Scholar 

  44. Zimmerli D, Brambillasca CS, Talens F, Bhin J, Linstra R, Romanens L, et al. MYC promotes immune-suppression in triple-negative breast cancer via inhibition of interferon signaling. Nat Commun. 2022;13:6579. https://doi.org/10.1038/s41467-022-34000-6.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  45. Sutherland C, Leighton IA, Cohen P. Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signaling. Biochem J. 1993;296:15–9. https://doi.org/10.1042/bj2960015.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  46. Frame S, Cohen P. GSK3 takes center stage more than 20 years after its discovery. Biochem J. 2001;359:1–16. https://doi.org/10.1042/0264-6021:3590001.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  47. Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature. 1995;378:785–9. https://doi.org/10.1038/378785a0.

    Article  PubMed  CAS  Google Scholar 

  48. Holm CK, Jensen SB, Jakobsen MR, Cheshenko N, Horan KA, Moeller HB, et al. Virus‒cell fusion as a trigger of innate immunity dependent on the adaptor STING. Nat Immunol. 2012;13:737–43. https://doi.org/10.1038/ni.2350.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  49. Tetzlaff MT, Yu W, Li M, Zhang P, Finegold M, Mahon K, et al. Defective cardiovascular development and elevated cyclin E and Notch proteins in mice lacking the Fbw7 F-box protein. Proc Natl Acad Sci USA. 2004;101:3338–45. https://doi.org/10.1073/pnas.0307875101.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  50. Zhang ZD, Zhong B. Regulation and function of the cGAS-MITA/STING axis in health and disease. Cell Insight. 2022;1:100001. https://doi.org/10.1016/j.cellin.2021.100001.

    Article  PubMed  PubMed Central  Google Scholar 

  51. Lin J, Song T, Li C, Mao W. GSK-3β in DNA repair, apoptosis, and resistance of chemotherapy, radiotherapy of cancer. Biochim Biophys Acta Mol Cell Res. 2020;1867:118659. https://doi.org/10.1016/j.bbamcr.2020.118659.

    Article  PubMed  CAS  Google Scholar 

  52. Pecoraro C, Faggion B, Balboni B, Carbone D, Peters GJ, Diana P, et al. GSK3β as a novel promising target to overcome chemoresistance in pancreatic cancer. Drug Resist Updat. 2021;58:100779. https://doi.org/10.1016/j.drup.2021.100779.

    Article  PubMed  CAS  Google Scholar 

  53. Ngamsiri P, Watcharasit P, Satayavivad J. Glycogen synthase kinase-3 (GSK3) controls deoxyglucose-induced mitochondrial biogenesis in human neuroblastoma SH-SY5Y cells. Mitochondrion. 2014;14:54–63. https://doi.org/10.1016/j.mito.2013.11.003.

    Article  PubMed  CAS  Google Scholar 

  54. Niculescu F, Nguyen P, Niculescu T, Rus H, Rus V, Via CS. Pathogenic T cells in murine lupus exhibit spontaneous signaling activity through phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways. Arthritis Rheum. 2003;48:1071–9. https://doi.org/10.1002/art.10900.

    Article  PubMed  CAS  Google Scholar 

  55. Tang H, Tan G, Guo Q, Pang R, Zeng F. Abnormal activation of the Akt-GSK3beta signaling pathway in peripheral blood T cells from patients with systemic lupus erythematosus. Cell Cycle. 2009;8:2789–93. https://doi.org/10.4161/cc.8.17.9446.

    Article  PubMed  CAS  Google Scholar 

  56. Chong Z, Bao C, He J, Chen T, Zhong L, Li G, et al. E3 ligase FBXW7 aggravates TMPD-induced systemic lupus erythematosus by promoting apoptosis. Cell Mol Immunol. 2018;15:1057–70. https://doi.org/10.1038/s41423-018-0167-z.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  57. Schoggins JW. Interferon-Stimulated Genes: What Do They All Do?. Annu Rev Virol. 2019;6:567–84. https://doi.org/10.1146/annurev-virology-092818-015756.

    Article  PubMed  CAS  Google Scholar 

  58. Hu MM, Liao CY, Yang Q, Xie XQ, Shu HB. Innate immunity to RNA virus is regulated by temporal and reversible sumoylation of RIG-I and MDA5. J Exp Med. 2017;214:973–89. https://doi.org/10.1084/jem.20161015.

    Article  PubMed  PubMed Central  CAS  Google Scholar 

  59. Hu MM, Yang Q, Xie XQ, Liao CY, Lin H, Liu TT, et al. Sumoylation Promotes the Stability of the DNA Sensor cGAS and the Adaptor STING to Regulate the Kinetics of Response to DNA Virus. Immunity. 2016;45:555–69. https://doi.org/10.1016/j.immuni.2016.08.014.

    Article  PubMed  CAS  Google Scholar 

  60. Morré DM, Morre DJ. Aqueous two-phase partition applied to the isolation of plasma membranes and Golgi apparatus from cultured mammalian cells. J Chromatogr B Biomed Sci Appl. 2000;743:377–87. https://doi.org/10.1016/s0378-4347(00)00058-x.

    Article  PubMed  Google Scholar 

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Acknowledgements

We are thankful for the support of the Instrument Sharing Center of the Medical Research Institute of Wuhan University.

Funding

This work was supported by grants from the State Key R&D Program of China (2022YFA1304900 and 2021YFA1302400), the Major Project of Guangzhou National Laboratory (GZNL2024A01016), the National Natural Science Foundation of China (32188101, 32470760 and 32170713 and 82404775), the CAMS Innovation Fund for Medical Sciences (2019-I2M-5-071), the Fundamental Research Funds for the Central Universities (2042022dx0003, 2042025kf0038), and the Translational Medicine and Interdisciplinary Research Joint Fund of Zhongnan Hospital of Wuhan University (Grant No. ZNJC202205).

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Authors and Affiliations

  1. Department of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University; Frontier Science Center for Immunology; Taikang Center for Life and Medical Sciences; State Key Laboratory of Virology; Institute of Hepatobiliary Diseases of Wuhan University, Wuhan, Hubei, 430071, China

    Xue-Dan Sun, Jia-Li Wang, Xin-Yu Zhang, Zi-Lun Ruan, Wei Liang, Qing Yang, Ling Li, Hong-Bing Shu & Ming-Ming Hu

  2. School of Basic Medical Sciences, Xianning Medical College, Hubei University of Science and Technology, Xianning, 437100, China

    Yi Guo

  3. The First Clinical College of Wuhan University, Wuhan, Hubei, China

    Wei-Tao Guan

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Contributions

M.M.H., H.B.S., L.L., and X.D.S. conceived and designed the study; X.D.S., J.L.W., X.Y.Z., Z.L.R., Y.G., W.L., and W.T.G. performed the experiments; X.D.S., M.M.H., H.B.S.L.L. and Q.Y. analyzed all the experimental data. M.M.H., H.B.S., L.L. and Q.Y. wrote the manuscript.

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Correspondence to Ling Li, Hong-Bing Shu or Ming-Ming Hu.

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Sun, XD., Wang, JL., Zhang, XY. et al. FBXW7 is a multifaceted regulator of the innate immune response to DNA viruses. Cell Mol Immunol 22, 1427–1443 (2025). https://doi.org/10.1038/s41423-025-01336-0

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