KAP1/TRIM28; innate immunity; post-translational modifications; transcriptional regulation; viral latency; virus–host interaction; Tripartite Motif-Containing Protein 28; TRIM28 protein, human; Humans; Animals; SARS-CoV-2/immunology; Influenza A virus/immunology; Protein Processing, Post-Translational; Host-Pathogen Interactions/immunology; Retroviridae/immunology; Tripartite Motif-Containing Protein 28/immunology; Tripartite Motif-Containing Protein 28/metabolism; Tripartite Motif-Containing Protein 28/genetics; Virus Diseases/immunology; Virus Diseases/virology; Host-Pathogen Interactions; Influenza A virus; Retroviridae; SARS-CoV-2; Virus Diseases; Microbiology; Immunology; Microbiology (medical); Infectious Diseases
Abstract :
[en] Krüppel-associated box (KRAB)-associated protein 1 (KAP1), also known as TRIM28 due to its tripartite motif (TRIM) domain, is a member of the transcription intermediary factor 1 (TIF1) family. Since its discovery in 1996, KAP1 has been widely studied as a scaffold protein involved in histone methylation, heterochromatin formation, and genome maintenance. Its function and stability are dynamically regulated by post-translational modifications (PTMs), including phosphorylation, SUMOylation, and acetylation. In addition, KAP1 serves as a signal transducer via its SUMO/ubiquitin E3 ligase activity. This review summarizes current advances in understanding the roles of KAP1 in regulating retroviruses (RVs), herpesviruses, and emerging respiratory viruses such as Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and influenza A virus (IAV), with a particular focus on the interplay between its structural domains and physiological functions. Recent findings on human immunodeficiency virus (HIV) are highlighted to address ongoing mechanistic controversies, particularly those involving KAP1-mediated latency control. We further examine novel insights into KAP1's involvement in other viruses, including hepatitis B virus (HBV), porcine reproductive and respiratory syndrome virus (PRRSV), and African swine fever virus (ASFV). as well as its emerging regulatory roles in host innate immune responses through PTM-mediated modulation of antiviral signaling pathways. Although KAP1 exerts both antiviral and proviral effects, the underlying mechanisms remain incompletely defined, especially in systems where conflicting observations exist for the same pathogen. These discrepancies-reflecting both methodological variation and KAP1's inherent regulatory complexity-underscore the need for deeper mechanistic insight. Future studies utilizing precise genetic tools and in vivo models will be critical for elucidating the context-specific roles of KAP1 in viral gene regulation and advancing its translational potential.
Disciplines :
Veterinary medicine & animal health
Author, co-author :
Xin, Ruihua ; Université de Liège - ULiège > TERRA Research Centre ; Key Laboratory of Veterinary Pharmaceutical Development of Ministry of Agriculture, Technology Innovation Center of Traditional Chinese Veterinary Medicine of Gansu Province, Lanzhou Institute of Husbandry and Pharmaceutical Sciences, Chinese Academy of Agricultural Sciences, Lanzhou, China
Garigliany, Mutien-Marie ; Université de Liège - ULiège > Département de morphologie et pathologie (DMP) > Pathologie générale et autopsies
Li, Jianxi; Key Laboratory of Veterinary Pharmaceutical Development of Ministry of Agriculture, Technology Innovation Center of Traditional Chinese Veterinary Medicine of Gansu Province, Lanzhou Institute of Husbandry and Pharmaceutical Sciences, Chinese Academy of Agricultural Sciences, Lanzhou, China
Language :
English
Title :
KAP1 in antiviral immunity: dual roles in viral silencing and immune regulation.
The author(s) declare financial support was received for the research and/or publication of this article. This work was supported by Science and Technology Innovation Project of the Chinese Academy of Agricultural Sciences (25-LZIHPS-06), Agricultural Science and Technology Support Project of Gansu Province (KJZC-2024-32), Key Research and Development Fund of Gansu Province (23YFNA0010), Lanzhou Science and Technology Project (2025-2-21).
Acharya A. Ambikan A. T. Thurman M. Malik M. R. Dyavar S. R. Végvári Á. et al. (2023). Proteomic landscape of astrocytes and pericytes infected with HIV/SARS-CoV-2 mono/co-infection, impacting on neurological complications. rs.3.rs-3031591. doi: 10.21203/rs.3.rs-3031591/v1, PMID: 37398206
Ait-Ammar A. Bellefroid M. Daouad F. Martinelli V. Van Assche J. Wallet C. et al. (2021). Inhibition of HIV-1 gene transcription by KAP1 in myeloid lineage. Sci. Rep. 11, 2692. doi: 10.1038/s41598-021-82164-w, PMID: 33514850
Ak A. K. Bhutta B. S. Mendez M. D. (2025). “Herpes simplex encephalitis,” in StatPearls (StatPearls Publishing, Treasure Island (FL). Available online at: http://www.ncbi.nlm.nih.gov/books/NBK557643/.
Ali S. R. Jordan M. Nagarajan P. Amit M. (2022). Nerve density and neuronal biomarkers in cancer. Cancers 14, 4817. doi: 10.3390/cancers14194817, PMID: 36230740
Allouch A. Di Primio C. Alpi E. Lusic M. Arosio D. Giacca M. et al. (2011). The TRIM family protein KAP1 inhibits HIV-1 integration. Cell Host Microbe 9, 484–495. doi: 10.1016/j.chom.2011.05.004, PMID: 21669397
Ashraf U. M. Abokor A. A. Edwards J. M. Waigi E. W. Royfman R. S. Hasan S. A.-M. et al. (2021). SARS-CoV-2, ACE2 expression, and systemic organ invasion. Physiol. Genomics 53, 51–60. doi: 10.1152/physiolgenomics.00087.2020, PMID: 33275540
Asimi V. Sampath Kumar A. Niskanen H. Riemenschneider C. Hetzel S. Naderi J. et al. (2022). Hijacking of transcriptional condensates by endogenous retroviruses. Nat. Genet. 54, 1238–1247. doi: 10.1038/s41588-022-01132-w, PMID: 35864192
Bacon C. W. Challa A. Hyder U. Shukla A. Borkar A. N. Bayo J. et al. (2020). KAP1 is a chromatin reader that couples steps of RNA polymerase II transcription to sustain oncogenic programs. Mol. Cell 78, 1133–1151.e14. doi: 10.1016/j.molcel.2020.04.024, PMID: 32402252
Ballmer D. Tardat M. Ortiz R. Graff-Meyer A. Ozonov E. A. Genoud C. et al. (2023). HP1 proteins regulate nucleolar structure and function by secluding pericentromeric constitutive heterochromatin. Nucleic Acids Res. 51, 117–143. doi: 10.1093/nar/gkac1159, PMID: 36533441
Barde I. Rauwel B. Marin-Florez R. M. Corsinotti A. Laurenti E. Verp S. et al. (2013). A KRAB/KAP1-miRNA cascade regulates erythropoiesis through stage-specific control of mitophagy. Science 340, 350–353. doi: 10.1126/science.1232398, PMID: 23493425
Bentz G. L. Moss C. R. Whitehurst C. B. Moody C. A. Pagano J. S. (2015). LMP1-induced sumoylation influences the maintenance of epstein-barr virus latency through KAP1. J. Virol. 89, 7465–7477. doi: 10.1128/JVI.00711-15, PMID: 25948750
Bhaduri-McIntosh S. Rousseau B. A. (2024). KAP1/TRIM28 – antiviral and proviral protagonist of herpesvirus biology. Trends Microbiol. 32, 1179–1189. doi: 10.1016/j.tim.2024.05.007, PMID: 38871562
Bhatia N. Xiao T. Z. Rosenthal K. A. Siddiqui I. A. Thiyagarajan S. Smart B. et al. (2013). MAGE-C2 promotes growth and tumorigenicity of melanoma cells, phosphorylation of KAP1, and DNA damage repair. J. Invest. Dermatol. 133, 759–767. doi: 10.1038/jid.2012.355, PMID: 23096706
Bojkowska K. Aloisio F. Cassano M. Kapopoulou A. De Sio F. S. Zangger N. et al. (2012). Liver-specific ablation of Krüppel-associated box–associated protein 1 in mice leads to male-predominant hepatosteatosis and development of liver adenoma. Hepatology 56, 1279–1290. doi: 10.1002/hep.25767, PMID: 22684873
Bolderson E. Savage K. I. Mahen R. Pisupati V. Graham M. E. Richard D. J. et al. (2012). Krüppel-associated box (KRAB)-associated co-repressor (KAP-1) ser-473 phosphorylation regulates heterochromatin protein 1β (HP1-β) mobilization and DNA repair in heterochromatin. J. Biol. Chem. 287, 28122–28131. doi: 10.1074/jbc.M112.368381, PMID: 22715096
Bove R. Sutton P. Nicholas J. (2024). Women’s health and pregnancy in multiple sclerosis. Neurologic Clinics 42, 275–293. doi: 10.1016/j.ncl.2023.07.004, PMID: 37980119
Brattås P. L. Jönsson M. E. Fasching L. Nelander Wahlestedt J. Shahsavani M. Falk R. et al. (2017). TRIM28 controls a gene regulatory network based on endogenous retroviruses in human neural progenitor cells. Cell Rep. 18, 1–11. doi: 10.1016/j.celrep.2016.12.010, PMID: 28052240
Bren I. Tal A. Strauss C. Schlesinger S. (2024). The role of Smarcad1 in retroviral repression in mouse embryonic stem cells. Mobile DNA 15, 4. doi: 10.1186/s13100-024-00314-z, PMID: 38468276
Broussard G. Damania B. (2020). Regulation of KSHV latency and lytic reactivation. Viruses 12, 1034. doi: 10.3390/v12091034, PMID: 32957532
Bunch H. Calderwood S. K. (2015). TRIM28 as a novel transcriptional elongation factor. BMC Mol. Biol. 16, 14. doi: 10.1186/s12867-015-0040-x, PMID: 26293668
Bürck C. Mund A. Berscheminski J. Kieweg L. Müncheberg S. Dobner T. et al. (2016). KAP1 is a host restriction factor that promotes human adenovirus E1B-55K SUMO modification. J. Virol. 90, 930–946. doi: 10.1128/JVI.01836-15, PMID: 26537675
Burton E. M. Akinyemi I. A. Frey T. R. Xu H. Li X. Su L. J. et al. (2021). A heterochromatin inducing protein differentially recognizes self versus foreign genomes. PloS Pathog. 17, e1009447. doi: 10.1371/journal.ppat.1009447, PMID: 33730092
Burton E. M. Goldbach-Mansky R. Bhaduri-McIntosh S. (2020). A promiscuous inflammasome sparks replication of a common tumor virus. Proc. Natl. Acad. Sci. U.S.A. 117, 1722–1730. doi: 10.1073/pnas.1919133117, PMID: 31919284
Cammas F. Mark M. Dollé P. Dierich A. Chambon P. Losson R. (2000). Mice lacking the transcriptional corepressor TIF1β are defective in early postimplantation development. Development 127, 2955–2963. doi: 10.1242/dev.127.13.2955, PMID: 10851139
Cao X. Chen Y. Chen Y. Jiang M. (2024). The role of tripartite motif family proteins in chronic liver diseases: molecular mechanisms and therapeutic potential. Biomolecules 14, 1038. doi: 10.3390/biom14081038, PMID: 39199424
Carusillo A. Mussolino C. (2020). DNA damage: from threat to treatment. Cells 9, 1665. doi: 10.3390/cells9071665, PMID: 32664329
Chang C.-W. Chou H.-Y. Lin Y.-S. Huang K.-H. Chang C.-J. Hsu T.-C. et al. (2008). Phosphorylation at Ser473 regulates heterochromatin protein 1 binding and corepressor function of TIF1beta/KAP1. BMC Mol. Biol. 9, 61. doi: 10.1186/1471-2199-9-61, PMID: 18590578
Chang P.-C. Fitzgerald L. D. Van Geelen A. Izumiya Y. Ellison T. J. Wang D.-H. et al. (2009). Kruppel-associated box domain-associated protein-1 as a latency regulator for kaposi’s sarcoma-associated herpesvirus and its modulation by the viral protein kinase. Cancer Res. 69, 5681–5689. doi: 10.1158/0008-5472.CAN-08-4570, PMID: 19584288
Chang J. Hwang H. J. Kim B. Choi Y.-G. Park J. Park Y. et al. (2021). TRIM28 functions as a negative regulator of aggresome formation. Autophagy 17, 4231–4248. doi: 10.1080/15548627.2021.1909835, PMID: 33783327
Chelmicki T. Roger E. Teissandier A. Dura M. Bonneville L. Rucli S. et al. (2021). m6A RNA methylation regulates the fate of endogenous retroviruses. Nature 591, 312–316. doi: 10.1038/s41586-020-03135-1, PMID: 33442060
Chen Y.-Y. Ran X.-H. Ni R.-Z. Mu D. (2023). TRIM28 negatively regulates the RLR signaling pathway by targeting MAVS for degradation via K48-linked polyubiquitination. J. Biol. Chem. 299, 104660. doi: 10.1016/j.jbc.2023.104660, PMID: 37119745
Cheng C.-T. (2014). KAPtain in charge of multiple missions: Emerging roles of KAP1. WJBC 5, 308. doi: 10.4331/wjbc.v5.i3.308, PMID: 25225599
Chikuma S. Suita N. Okazaki I.-M. Shibayama S. Honjo T. (2012). TRIM28 prevents autoinflammatory T cell development in vivo. Nat. Immunol. 13, 596–603. doi: 10.1038/ni.2293, PMID: 22544392
Chikuma S. Yamanaka S. Nakagawa S. Ueda M. T. Hayabuchi H. Tokifuji Y. et al. (2021). TRIM28 expression on dendritic cells prevents excessive T cell priming by silencing endogenous retrovirus. J. Immunol. 206, 1528–1539. doi: 10.4049/jimmunol.2001003, PMID: 33619215
Chou T. C. Maggirwar N. S. Marsden M. D. (2024). HIV persistence, latency, and cure approaches: where are we now? Viruses 16, 1163. doi: 10.3390/v16071163, PMID: 39066325
Cohen J. I. (2020). Herpesvirus latency. J. Clin. Invest. 130, 3361–3369. doi: 10.1172/JCI136225, PMID: 32364538
Crawford K. Lager K. M. Kulshreshtha V. Miller L. C. Faaberg K. S. (2016). Status of vaccines for porcine epidemic diarrhea virus in the United States and Canada. Virus Res. 226, 108–116. doi: 10.1016/j.virusres.2016.08.005, PMID: 27545066
Cui Z. Zhou L. Zhao S. Li W. Li J. Chen J. et al. (2023). The host E3-ubiquitin ligase TRIM28 impedes viral protein GP4 ubiquitination and promotes PRRSV replication. IJMS 24, 10965. doi: 10.3390/ijms241310965, PMID: 37446143
Czerwińska P. Mazurek S. Wiznerowicz M. (2017). The complexity of TRIM28 contribution to cancer. J. BioMed. Sci. 24, 63. doi: 10.1186/s12929-017-0374-4, PMID: 28851455
D’Orso I. (2016). 7SKiing on chromatin: Move globally, act locally. RNA Biol. 13, 545–553. doi: 10.1080/15476286.2016.1181254, PMID: 27128603
Da Costa I. C. Schmidt C. K. (2020). Ubiquitin-like proteins in the DNA damage response: the next generation. Essays Biochem. 64, 737–752. doi: 10.1042/EBC20190095, PMID: 32451552
Damania B. Kenney S. C. Raab-Traub N. (2022). Epstein-Barr virus: Biology and clinical disease. Cell 185, 3652–3670. doi: 10.1016/j.cell.2022.08.026, PMID: 36113467
De La Cruz-Herrera C. F. Tatham M. H. Siddiqi U. Z. Shire K. Marcon E. Greenblatt J. F. et al. (2023). Changes in SUMO-modified proteins in Epstein-Barr virus infection identifies reciprocal regulation of TRIM24/28/33 complexes and the lytic switch BZLF1. PloS Pathog. 19, e1011477. doi: 10.1371/journal.ppat.1011477, PMID: 37410772
Dobson R. Giovannoni G. (2019). Multiple sclerosis – a review. Euro J. Neurol. 26, 27–40. doi: 10.1111/ene.13819, PMID: 30300457
Ecco G. Imbeault M. Trono D. (2017). KRAB zinc finger proteins. Development 144, 2719–2729. doi: 10.1242/dev.132605, PMID: 28765213
Elsässer S. J. Noh K.-M. Diaz N. Allis C. D. Banaszynski L. A. (2015). Histone H3.3 is required for endogenous retroviral element silencing in embryonic stem cells. Nature 522, 240–244. doi: 10.1038/nature14345, PMID: 25938714
Enriquez-Gasca R. Gould P. A. Tunbak H. Conde L. Herrero J. Chittka A. et al. (2023). Co-option of endogenous retroviruses through genetic escape from TRIM28 repression. Cell Rep. 42, 112625. doi: 10.1016/j.celrep.2023.112625, PMID: 37294634
Fasching L. Kapopoulou A. Sachdeva R. Petri R. Jönsson M. E. Männe C. et al. (2015). TRIM28 represses transcription of endogenous retroviruses in neural progenitor cells. Cell Rep. 10, 20–28. doi: 10.1016/j.celrep.2014.12.004, PMID: 25543143
Feng H. Yi R. Wu S. Wang G. Sun R. Lin L. et al. (2022). KAP1 positively modulates influenza A virus replication by interacting with PB2 and NS1 proteins in human lung epithelial cells. Viruses 14, 689. doi: 10.3390/v14040689, PMID: 35458419
Fonti G. Marcaida M. J. Bryan L. C. Träger S. Kalantzi A. S. Helleboid P.-Y. J. et al. (2019). KAP1 is an antiparallel dimer with a functional asymmetry. Life Sci. Alliance 2, e201900349. doi: 10.26508/lsa.201900349, PMID: 31427381
Forte E. Swaminathan S. Schroeder M. W. Kim J. Y. Terhune S. S. Hummel M. (2018). Tumor necrosis factor alpha induces reactivation of human cytomegalovirus independently of myeloid cell differentiation following posttranscriptional establishment of latency. mBio 9, e01560–e01518. doi: 10.1128/mBio.01560-18, PMID: 30206173
Friedman J. R. Fredericks W. J. Jensen D. E. Speicher D. W. Huang X. P. Neilson E. G. et al. (1996). KAP-1, a novel corepressor for the highly conserved KRAB repression domain. Genes Dev. 10, 2067–2078. doi: 10.1101/gad.10.16.2067, PMID: 8769649
Fukuda K. Shinkai Y. (2020). SETDB1-mediated silencing of retroelements. Viruses 12, 596. doi: 10.3390/v12060596, PMID: 32486217
Gan J. Wang C. Jin Y. Guo Y. Xu F. Zhu Q. et al. (2015). Proteomic profiling identifies the SIM-associated complex of KSHV-encoded LANA. Proteomics 15, 2023–2037. doi: 10.1002/pmic.201400624, PMID: 25894481
Gao X. Li Q. Chen G. He H. Ma Y. (2020). MAGEA3 promotes proliferation and suppresses apoptosis in cervical cancer cells by inhibiting the KAP1/p53 signaling pathway. Am. J. Transl. Res. 12, 3596–3612., PMID: 32774721
Gao F. Wen G. (2025). Strategies and scheming: the war between PRRSV and host cells. Virol. J. 22, 191. doi: 10.1186/s12985-025-02685-y, PMID: 40500743
Gareau J. R. Lima C. D. (2010). The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11, 861–871. doi: 10.1038/nrm3011, PMID: 21102611
Garigliany M. Van Laere A.-S. Clercx C. Giet D. Escriou N. Huon C. et al. (2020). SARS-CoV-2 natural transmission from human to cat, Belgium, march 2020. Emerg. Infect. Dis. 26, 3069–3071. doi: 10.3201/eid2612.202223, PMID: 32788033
Geis F. K. Goff S. P. (2020). Silencing and transcriptional regulation of endogenous retroviruses: an overview. Viruses 12, 884. doi: 10.3390/v12080884, PMID: 32823517
Germini D. Sall F. B. Shmakova A. Wiels J. Dokudovskaya S. Drouet E. et al. (2020). Oncogenic properties of the EBV ZEBRA protein. Cancers (Basel) 12, 1479. doi: 10.3390/cancers12061479, PMID: 32517128
Gjyshi O. Roy A. Dutta S. Veettil M. V. Dutta D. Chandran B. (2015). Activated nrf2 interacts with kaposi’s sarcoma-associated herpesvirus latency protein LANA-1 and host protein KAP1 to mediate global lytic gene repression. J. Virol. 89, 7874–7892. doi: 10.1128/JVI.00895-15, PMID: 25995248
Goodarzi A. A. Kurka T. Jeggo P. A. (2011). KAP-1 phosphorylation regulates CHD3 nucleosome remodeling during the DNA double-strand break response. Nat. Struct. Mol. Biol. 18, 831–839. doi: 10.1038/nsmb.2077, PMID: 21642969
Greenwood A. D. Ishida Y. O’Brien S. P. Roca A. L. Eiden M. V. (2018). Transmission, evolution, and endogenization: lessons learned from recent retroviral invasions. Microbiol. Mol. Biol. Rev. 82, e00044–e00017. doi: 10.1128/MMBR.00044-17, PMID: 29237726
Grewal S. I. S. (2023). The molecular basis of heterochromatin assembly and epigenetic inheritance. Mol. Cell 83, 1767–1785. doi: 10.1016/j.molcel.2023.04.020, PMID: 37207657
Griffiths P. Reeves M. (2021). Pathogenesis of human cytomegalovirus in the immunocompromised host. Nat. Rev. Microbiol. 19, 759–773. doi: 10.1038/s41579-021-00582-z, PMID: 34168328
Gugliesi F. Pasquero S. Griffante G. Scutera S. Albano C. Pacheco S. F. C. et al. (2021). Human cytomegalovirus and autoimmune diseases: where are we? Viruses 13, 260. doi: 10.3390/v13020260, PMID: 33567734
Haggerty C. Kretzmer H. Riemenschneider C. Kumar A. S. Mattei A. L. Bailly N. et al. (2021). Dnmt1 has de novo activity targeted to transposable elements. Nat. Struct. Mol. Biol. 28, 594–603. doi: 10.1038/s41594-021-00603-8, PMID: 34140676
Hale B. G. (2022). Antiviral immunity triggered by infection-induced host transposable elements. Curr. Opin. Virol. 52, 211–216. doi: 10.1016/j.coviro.2021.12.006, PMID: 34959082
Harms P. W. Harms K. L. Moore P. S. DeCaprio J. A. Nghiem P. Wong M. K. K. et al. (2018). The biology and treatment of Merkel cell carcinoma: current understanding and research priorities. Nat. Rev. Clin. Oncol. 15, 763–776. doi: 10.1038/s41571-018-0103-2, PMID: 30287935
Harrison K. S. Jones C. (2022). Regulation of herpes simplex virus type 1 latency-reactivation cycle and ocular disease by cellular signaling pathways. Exp. Eye Res. 218, 109017. doi: 10.1016/j.exer.2022.109017, PMID: 35240194
Hosoya T. Clifford M. Losson R. Tanabe O. Engel J. D. (2013). TRIM28 is essential for erythroblast differentiation in the mouse. Blood 122, 3798–3807. doi: 10.1182/blood-2013-04-496166, PMID: 24092935
Hu C. Zhang S. Gao X. Gao X. Xu X. Lv Y. et al. (2012). Roles of kruppel-associated box (KRAB)-associated co-repressor KAP1 ser-473 phosphorylation in DNA damage response. J. Biol. Chem. 287, 18937–18952. doi: 10.1074/jbc.M111.313262, PMID: 22496453
Hua F. Nass T. Parvatiyar K. (2024). TRIM28 facilitates type I interferon activation by targeting TBK1. Front. Immunol. 15. doi: 10.3389/fimmu.2024.1279920, PMID: 38495890
Huang R.-X. Zhou P.-K. (2020). DNA damage response signaling pathways and targets for radiotherapy sensitization in cancer. Sig Transduct Target Ther. 5, 60. doi: 10.1038/s41392-020-0150-x, PMID: 32355263
Hughes S. H. (2015). Reverse transcription of retroviruses and LTR retrotransposons. Microbiol. Spectr. 3, 3.2.18. doi: 10.1128/microbiolspec.MDNA3-0027-2014, PMID: 26104704
Ivanov A. V. Peng H. Yurchenko V. Yap K. L. Negorev D. G. Schultz D. C. et al. (2007). PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing. Mol. Cell 28, 823–837. doi: 10.1016/j.molcel.2007.11.012, PMID: 18082607
Iyengar S. Farnham P. J. (2011). KAP1 protein: an enigmatic master regulator of the genome. J. Biol. Chem. 286, 26267–26276. doi: 10.1074/jbc.R111.252569, PMID: 21652716
Iyengar S. Ivanov A. V. Jin V. X. Rauscher F. J. Farnham P. J. (2011). Functional analysis of KAP1 genomic recruitment. Mol. Cell. Biol. 31, 1833–1847. doi: 10.1128/MCB.01331-10, PMID: 21343339
Jackson C. B. Farzan M. Chen B. Choe H. (2022). Mechanisms of SARS-CoV-2 entry into cells. Nat. Rev. Mol. Cell Biol. 23, 3–20. doi: 10.1038/s41580-021-00418-x, PMID: 34611326
Jakobsson J. Cordero M. I. Bisaz R. Groner A. C. Busskamp V. Bensadoun J.-C. et al. (2008). KAP1-mediated epigenetic repression in the forebrain modulates behavioral vulnerability to stress. Neuron 60, 818–831. doi: 10.1016/j.neuron.2008.09.036, PMID: 19081377
Jang S.-H. Choi H.-W. Ahn J. Jang S. Yoon J.-H. Lee M.-G. et al. (2024). XAF1 antagonizes TRIM28 activity through the assembly of a ZNF313-mediated destruction complex to suppress tumor Malignancy. Mol. BioMed. 5, 58. doi: 10.1186/s43556-024-00224-9, PMID: 39532800
Jovčevska I. Zupanec N. Urlep Ž. Vranič A. Matos B. Stokin C. L. et al. (2017). Differentially expressed proteins in glioblastoma multiforme identified with a nanobody-based anti-proteome approach and confirmed by OncoFinder as possible tumor-class predictive biomarker candidates. Oncotarget 8, 44141–44158. doi: 10.18632/oncotarget.17390, PMID: 28498803
Jung K. Saif L. J. Wang Q. (2020). Porcine epidemic diarrhea virus (PEDV): An update on etiology, transmission, pathogenesis, and prevention and control. Virus Res. 286, 198045. doi: 10.1016/j.virusres.2020.198045, PMID: 32502552
Kajon A. E. (2024). Adenovirus infections: new insights for the clinical laboratory. J. Clin. Microbiol. 62, e0083622. doi: 10.1128/jcm.00836-22, PMID: 39189703
Kanda T. (2018). “EBV-encoded latent genes,” in Human Herpesviruses. Eds. Kawaguchi Y. Mori Y. Kimura H. (Springer Singapore, Singapore), 377–394. doi: 10.1007/978-981-10-7230-7_17, PMID: 29896676
Kawabe H. Stegmüller J. (2021). The role of E3 ubiquitin ligases in synapse function in the healthy and diseased brain. Mol. Cell. Neurosci. 112, 103602. doi: 10.1016/j.mcn.2021.103602, PMID: 33581237
Khetchoumian K. Teletin M. Mark M. Lerouge T. Cerviño M. Oulad-Abdelghani M. et al. (2004). TIF1δ, a novel HP1-interacting member of the transcriptional intermediary factor 1 (TIF1) family expressed by elongating spermatids. J. Biol. Chem. 279, 48329–48341. doi: 10.1074/jbc.M404779200, PMID: 15322135
Kim S.-S. Chen Y.-M. O’Leary E. Witzgall R. Vidal M. Bonventre J. V. (1996). A novel member of the RING finger family, KRIP-1, associates with the KRAB-A transcriptional repressor domain of zinc finger proteins. Proc. Natl. Acad. Sci. U.S.A. 93, 15299–15304. doi: 10.1073/pnas.93.26.15299, PMID: 8986806
Kimura Y. Nagao A. Fujioka Y. Satou A. Taira T. Iguchi-Ariga S. M. M. et al. (2007). MM-1 facilitates degradation of c-Myc by recruiting proteasome and a novel ubiquitin E3 ligase. Int. J. Oncol. 31, 829–836. doi: 10.3892/ijo.31.4.829, PMID: 17786314
King C. A. (2013). Kaposi’s sarcoma-associated herpesvirus kaposin B induces unique monophosphorylation of STAT3 at serine 727 and MK2-mediated inactivation of the STAT3 transcriptional repressor TRIM28. J. Virol. 87, 8779–8791. doi: 10.1128/JVI.02976-12, PMID: 23740979
King C. A. Li X. Barbachano-Guerrero A. Bhaduri-McIntosh S. (2015). STAT3 regulates lytic activation of kaposi’s sarcoma-associated herpesvirus. J. Virol. 89, 11347–11355. doi: 10.1128/JVI.02008-15, PMID: 26339061
Köcher S. Zech H. B. Krug L. Gatzemeier F. Christiansen S. Meyer F. et al. (2022). A lack of effectiveness in the ATM-orchestrated DNA damage response contributes to the DNA repair defect of HPV-positive head and neck cancer cells. Front. Oncol. 12. doi: 10.3389/fonc.2022.765968, PMID: 35719921
Kotobuki Y. Tonomura K. Fujimoto M. (2021). Transcriptional intermediary factor 1 (TIF1) and anti-TIF1γ antibody-positive dermatomyositis. Immunol. Med. 44, 23–29. doi: 10.1080/25785826.2020.1791402, PMID: 32649853
Krasnopolsky S. Kuzmina A. Taube R. (2020). Genome-wide CRISPR knockout screen identifies ZNF304 as a silencer of HIV transcription that promotes viral latency. PloS Pathog. 16, e1008834. doi: 10.1371/journal.ppat.1008834, PMID: 32956422
Krebs A.-S. Mendonça L. M. Zhang P. (2021). Structural analysis of retrovirus assembly and maturation. Viruses 14, 54. doi: 10.3390/v14010054, PMID: 35062258
Krischuns T. Günl F. Henschel L. Binder M. Willemsen J. Schloer S. et al. (2018). Phosphorylation of TRIM28 enhances the expression of IFN-β and proinflammatory cytokines during HPAIV infection of human lung epithelial cells. Front. Immunol. 9. doi: 10.3389/fimmu.2018.02229, PMID: 30323812
Kuang M. Zhao Y. Yu H. Li S. Liu T. Chen L. et al. (2023). XAF1 promotes anti-RNA virus immune responses by regulating chromatin accessibility. Sci. Adv. 9, eadg5211. doi: 10.1126/sciadv.adg5211, PMID: 37595039
Kuo C.-Y. Li X. Kong X.-Q. Luo C. Chang C.-C. Chung Y. et al. (2014). An arginine-rich motif of ring finger protein 4 (RNF4) oversees the recruitment and degradation of the phosphorylated and SUMOylated krüppel-associated box domain-associated protein 1 (KAP1)/TRIM28 protein during genotoxic stress. J. Biol. Chem. 289, 20757–20772. doi: 10.1074/jbc.M114.555672, PMID: 24907272
Kuo C.-Y. Li X. Stark J. M. Shih H.-M. Ann D. K. (2016). RNF4 regulates DNA double-strand break repair in a cell cycle-dependent manner. Cell Cycle 15, 787–798. doi: 10.1080/15384101.2016.1138184, PMID: 26766492
Lechner M. S. Begg G. E. Speicher D. W. Rauscher F. J. (2000). Molecular determinants for targeting heterochromatin protein 1-mediated gene silencing: direct chromoshadow domain–KAP-1 corepressor interaction is essential. Mol. Cell. Biol. 20, 6449–6465. doi: 10.1128/MCB.20.17.6449-6465.2000, PMID: 10938122
Lee A. CingÖz O. Sabo Y. Goff S. P. (2018). Characterization of interaction between Trim28 and YY1 in silencing proviral DNA of Moloney murine leukemia virus. Virology 516, 165–175. doi: 10.1016/j.virol.2018.01.012, PMID: 29407374
Lee D.-H. Goodarzi A. A. Adelmant G. O. Pan Y. Jeggo P. A. Marto J. A. et al. (2012). Phosphoproteomic analysis reveals that PP4 dephosphorylates KAP-1 impacting the DNA damage response: PP4 regulates KAP-1 function in DDR. EMBO J. 31, 2403–2415. doi: 10.1038/emboj.2012.86, PMID: 22491012
Lee Y.-K. Thomas S. N. Yang A. J. Ann D. K. (2007). Doxorubicin down-regulates krüppel-associated box domain-associated protein 1 sumoylation that relieves its transcription repression on p21WAF1/CIP1 in breast cancer MCF-7 cells. J. Biol. Chem. 282, 1595–1606. doi: 10.1074/jbc.M606306200, PMID: 17079232
Leonardi L. Rivalta B. Leone F. Cancrini C. Caffarelli C. Marseglia G. L. et al. (2022). Host defenses to viruses: lessons from inborn errors of immunity. Medicina 58, 248. doi: 10.3390/medicina58020248, PMID: 35208572
Li X. Burton E. M. Bhaduri-McIntosh S. (2017). Chloroquine triggers Epstein-Barr virus replication through phosphorylation of KAP1/TRIM28 in Burkitt lymphoma cells. PloS Pathog. 13, e1006249. doi: 10.1371/journal.ppat.1006249, PMID: 28249048
Li X. Burton E. M. Koganti S. Zhi J. Doyle F. Tenenbaum S. A. et al. (2018). KRAB-ZFP repressors enforce quiescence of oncogenic human herpesviruses. J. Virol. 92, e00298–e00218. doi: 10.1128/JVI.00298-18, PMID: 29695433
Li H. Chen M. Zheng T. Lei X. Lin C. Li S. et al. (2024a). IFITM1 and IFITM2 inhibit the replication of senecavirus A by positive feedback with RIG-I signaling pathway. Veterinary Microbiol. 292, 110050. doi: 10.1016/j.vetmic.2024.110050, PMID: 38484578
Li J. Cheng H. Zhao Y. Wang Y. Gong C. Gong R. et al. (2024b). ZNF331 represses the proliferation of head and neck squamous cell carcinoma via co-repressor TRIM28. Oral. Dis. 31, odi.15209. doi: 10.1111/odi.15209, PMID: 39587824
Li X. Kozlov S. V. El-Guindy A. Bhaduri-McIntosh S. (2019). Retrograde regulation by the viral protein kinase epigenetically sustains the epstein-barr virus latency-to-lytic switch to augment virus production. J. Virol. 93, e00572–e00519. doi: 10.1128/JVI.00572-19, PMID: 31189703
Li X. Lin H. H. Chen H. Xu X. Shih H.-M. Ann D. K. (2010). SUMOylation of the transcriptional co-repressor KAP1 is regulated by the serine and threonine phosphatase PP1. Sci. Signal. 3, ra32. doi: 10.1126/scisignal.2000781, PMID: 20424263
Li Q. Qin Y. Wang W. Jia M. Zhao W. Zhao C. (2021). KAP1-mediated epigenetic suppression in anti-RNA viral responses by direct targeting RIG-I and MDA5. J. Immunol. 207, 1903–1910. doi: 10.4049/jimmunol.2100342, PMID: 34497149
Li M. Xu X. Chang C.-W. Liu Y. (2020). TRIM28 functions as the SUMO E3 ligase for PCNA in prevention of transcription induced DNA breaks. Proc. Natl. Acad. Sci. U.S.A. 117, 23588–23596. doi: 10.1073/pnas.2004122117, PMID: 32900933
Li X. Yan Z. Ma J. Li G. Liu X. Peng Z. et al. (2024c). TRIM28 promotes porcine epidemic diarrhea virus replication by mitophagy-mediated inhibition of the JAK-STAT1 pathway. Int. J. Biol. Macromolecules 254, 127722. doi: 10.1016/j.ijbiomac.2023.127722, PMID: 37907173
Liang Q. Deng H. Li X. Wu X. Tang Q. Chang T.-H. et al. (2011). Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7. J. Immunol. 187, 4754–4763. doi: 10.4049/jimmunol.1101704, PMID: 21940674
Lin J. Guo D. Liu H. Zhou W. Wang C. Müller I. et al. (2021). The SETDB1–TRIM28 complex suppresses antitumor immunity. Cancer Immunol. Res. 9, 1413–1424. doi: 10.1158/2326-6066.CIR-21-0754, PMID: 34848497
Lin Y.-H. Yuan J. Pei H. Liu T. Ann D. K. Lou Z. (2015). KAP1 deacetylation by SIRT1 promotes non-homologous end-joining repair. PloS One 10, e0123935. doi: 10.1371/journal.pone.0123935, PMID: 25905708
Linney E. Davis B. Overhauser J. Chao E. Fan H. (1984). Non-function of a Moloney murine leukaemia virus regulatory sequence in F9 embryonal carcinoma cells. Nature 308, 470–472. doi: 10.1038/308470a0, PMID: 6323996
Lion T. (2014). Adenovirus infections in immunocompetent and immunocompromised patients. Clin. Microbiol. Rev. 27, 441–462. doi: 10.1128/CMR.00116-13, PMID: 24982316
Liu S. Cai X. Wu J. Cong Q. Chen X. Li T. et al. (2015). Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation. Science 347, aaa2630. doi: 10.1126/science.aaa2630, PMID: 25636800
Liu Y. Cao B. Hu L. Ye J. Tian W. He X. (2022). The dual roles of MAGE-C2 in p53 ubiquitination and cell proliferation through E3 ligases MDM2 and TRIM28. Front. Cell Dev. Biol. 10. doi: 10.3389/fcell.2022.922675, PMID: 35927984
Liu H. Chen H. Deng X. Peng Y. Zeng Q. Song Z. et al. (2019). Knockdown of TRIM28 inhibits PDGF-BB-induced vascular smooth muscle cell proliferation and migration. Chemico-Biological Interact. 311, 108772. doi: 10.1016/j.cbi.2019.108772, PMID: 31351049
Liu X. Gan J. Du S. Zhu C. Wang Y. Jia Y. et al. (2021b). Proteomic profiling identifies kaposi’s sarcoma-associated herpesvirus (KSHV)-encoded LANASIM -associated proteins in hypoxia. mSystems 6, e01109–e01121. doi: 10.1128/mSystems.01109-21, PMID: 34726485
Liu J. Gao M. He J. Wu K. Lin S. Jin L. et al. (2021a). The RNA m6A reader YTHDC1 silences retrotransposons and guards ES cell identity. Nature 591, 322–326. doi: 10.1038/s41586-021-03313-9, PMID: 33658714
Liu H.-L. Nan H. Zhao W.-W. Wan X.-B. Fan X.-J. (2024). Phase separation in DNA double-strand break response. Nucleus 15, 2296243. doi: 10.1080/19491034.2023.2296243, PMID: 38146123
Liu C. Zhao K. Chen Y. Yao Y. Tang J. Wang J. et al. (2023a). Mitochondrial glycerol-3-phosphate dehydrogenase restricts HBV replication via the TRIM28-mediated degradation of HBx. J. Virol. 97, e00580–e00523. doi: 10.1128/jvi.00580-23, PMID: 37166302
Liu W. Zhu Y. Ye W. Xiong J. Wang H. Gao Y. et al. (2025). Redox regulation of TRIM28 facilitates neuronal ferroptosis by promoting SUMOylation and inhibiting OPTN-selective autophagic degradation of ACSL4. Cell Death Differ 32, 1041–1057. doi: 10.1038/s41418-025-01452-4, PMID: 39875520
Liu F. Zhuang W. Song B. Yang Y. Liu J. Zheng Y. et al. (2023b). MAVS-loaded unanchored Lys63-linked polyubiquitin chains activate the RIG-I-MAVS signaling cascade. Cell Mol. Immunol. 20, 1186–1202. doi: 10.1038/s41423-023-01065-2, PMID: 37582970
Lobanova Y. Filonova G. Kaplun D. Zhigalova N. Prokhortchouk E. Zhenilo S. (2023). TRIM28 regulates transcriptional activity of methyl-DNA binding protein Kaiso by SUMOylation. Biochimie 206, 73–80. doi: 10.1016/j.biochi.2022.10.006, PMID: 36252888
Lork M. Lieber G. Hale B. G. (2021). Proteomic approaches to dissect host SUMOylation during innate antiviral immune responses. Viruses 13, 528. doi: 10.3390/v13030528, PMID: 33806893
Lu R. Zhao X. Li J. Niu P. Yang B. Wu H. et al. (2020). Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. Lancet 395, 565–574. doi: 10.1016/S0140-6736(20)30251-8, PMID: 32007145
Luo J. Zhang Y. Guo Y. Tang H. Wei H. Liu S. et al. (2017). TRIM28 regulates Igf2-H19 and Dlk1-Gtl2 imprinting by distinct mechanisms during sheep fibroblast proliferation. Gene 637, 152–160. doi: 10.1016/j.gene.2017.09.048, PMID: 28947302
Ma X. Yang T. Luo Y. Wu L. Jiang Y. Song Z. et al. (2019). TRIM28 promotes HIV-1 latency by SUMOylating CDK9 and inhibiting P-TEFb. eLife 8, e42426. doi: 10.7554/eLife.42426, PMID: 30652970
Margalit L. Strauss C. Tal A. Schlesinger S. (2020). Trim24 and trim33 play a role in epigenetic silencing of retroviruses in embryonic stem cells. Viruses 12, 1015. doi: 10.3390/v12091015, PMID: 32932986
McAvera R. M. Crawford L. J. (2020). TIF1 proteins in genome stability and cancer. Cancers 12, 2094. doi: 10.3390/cancers12082094, PMID: 32731534
McNamara R. P. Guzman C. Reeder J. E. D’Orso I. (2016a). Genome-wide analysis of KAP1, the 7SK snRNP complex, and RNA polymerase II. Genomics Data 7, 250–255. doi: 10.1016/j.gdata.2016.01.019, PMID: 26981421
McNamara R. P. Reeder J. E. McMillan E. A. Bacon C. W. McCann J. L. D’Orso I. (2016b). KAP1 recruitment of the 7SK snRNP complex to promoters enables transcription elongation by RNA polymerase II. Mol. Cell 61, 39–53. doi: 10.1016/j.molcel.2015.11.004, PMID: 26725010
Meroni G. Diez-Roux G. (2005). TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases. BioEssays 27, 1147–1157. doi: 10.1002/bies.20304, PMID: 16237670
Messerschmidt D. M. De Vries W. Ito M. Solter D. Ferguson-Smith A. Knowles B. B. (2012). Trim28 is required for epigenetic stability during mouse oocyte to embryo transition. Science 335, 1499–1502. doi: 10.1126/science.1216154, PMID: 22442485
Metzger M. B. Pruneda J. N. Klevit R. E. Weissman A. M. (2014). RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim. Biophys. Acta (BBA) - Mol. Cell Res. 1843, 47–60. doi: 10.1016/j.bbamcr.2013.05.026, PMID: 23747565
Miyazato P. Matsuo M. Katsuya H. Satou Y. (2016). Transcriptional and epigenetic regulatory mechanisms affecting HTLV-1 provirus. Viruses 8, 171. doi: 10.3390/v8060171, PMID: 27322309
Morii M. Kubota S. Iimori M. Yokomizo-Nakano T. Hamashima A. Bai J. et al. (2024). TIF1β activates leukemic transcriptional program in HSCs and promotes BCR::ABL1-induced myeloid leukemia. Leukemia 38, 1275–1286. doi: 10.1038/s41375-024-02276-w, PMID: 38734786
Morton E. L. Forst C. V. Zheng Y. DePaula-Silva A. B. Ramirez N.-G. P. Planelles V. et al. (2019). Transcriptional circuit fragility influences HIV proviral fate. Cell Rep. 27, 154–171.e9. doi: 10.1016/j.celrep.2019.03.007, PMID: 30943398
Nyenhuis D. A. Watanabe S. M. Tjandra N. Carter C. A. (2025). Tsg101 mimicry of canonical E2 enzymes underlies its role in ubiquitin signaling. Proc. Natl. Acad. Sci. U.S.A. 122, e2419542121. doi: 10.1073/pnas.2419542121, PMID: 39739800
Oksenych V. Kainov D. E. (2021). DNA damage response. Biomolecules 11, 123. doi: 10.3390/biom11010123, PMID: 33477863
Ouyang C. Lu G. He W. Bay B.-H. Shen H.-M. (2022). Post-translational modification in control of SIRT1 stability during DNA damage response. Int. J. Biol. Sci. 18, 2655–2669. doi: 10.7150/ijbs.68587, PMID: 35541916
Padeken J. Methot S. P. Gasser S. M. (2022). Establishment of H3K9-methylated heterochromatin and its functions in tissue differentiation and maintenance. Nat. Rev. Mol. Cell Biol. 23, 623–640. doi: 10.1038/s41580-022-00483-w, PMID: 35562425
Park H.-H. Kim H.-R. Park S.-Y. Hwang S.-M. Hong S. M. Park S. et al. (2021). RIPK3 activation induces TRIM28 derepression in cancer cells and enhances the anti-tumor microenvironment. Mol. Cancer 20, 107. doi: 10.1186/s12943-021-01399-3, PMID: 34419074
Pavlaki I. Alammari F. Sun B. Clark N. Sirey T. Lee S. et al. (2018). The long non-coding RNA Paupar promotes KAP 1-dependent chromatin changes and regulates olfactory bulb neurogenesis. EMBO J. 37, e98219. doi: 10.15252/embj.201798219, PMID: 29661885
Pellegrina D. Bahcheli A. T. Krassowski M. Reimand J. (2022). Human phospho-signaling networks of SARS-CoV-2 infection are rewired by population genetic variants. Mol. Syst. Biol. 18, e10823. doi: 10.15252/msb.202110823, PMID: 35579274
Peng H. Begg G. E. Schultz D. C. Friedman J. R. Jensen D. E. Speicher D. W. et al. (2000). Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions. J. Mol. Biol. 295, 1139–1162. doi: 10.1006/jmbi.1999.3402, PMID: 10653693
Peng H. Gibson L. C. Capili A. D. Borden K. L. B. Osborne M. J. Harper S. L. et al. (2007). The Structurally Disordered KRAB Repression Domain Is Incorporated into a Protease Resistant Core upon Binding to KAP-1-RBCC Domain. J. Mol. Biol. 370, 269–289. doi: 10.1016/j.jmb.2007.03.047, PMID: 17512541
Peng J. Wysocka J. (2008). It takes a PHD to SUMO. Trends Biochem. Sci. 33, 191–194. doi: 10.1016/j.tibs.2008.02.003, PMID: 18406149
Pisano G. Roy A. Ahmed Ansari M. Kumar B. Chikoti L. Chandran B. (2017). Interferon-γ-inducible protein 16 (IFI16) is required for the maintenance of Epstein-Barr virus latency. Virol. J. 14, 221. doi: 10.1186/s12985-017-0891-5, PMID: 29132393
Poole E. Sinclair J. (2022). Latency-associated upregulation of SERBP1 is important for the recruitment of transcriptional repressors to the viral major immediate early promoter of human cytomegalovirus during latent carriage. Front. Microbiol. 13. doi: 10.3389/fmicb.2022.999290, PMID: 36504797
Qin Y. Li Q. Liang W. Yan R. Tong L. Jia M. et al. (2021). TRIM28 SUMOylates and stabilizes NLRP3 to facilitate inflammasome activation. Nat. Commun. 12, 4794. doi: 10.1038/s41467-021-25033-4, PMID: 34373456
Randolph K. Hyder U. Challa A. Perez E. D’Orso I. (2024). Functional analysis of KAP1/TRIM28 requirements for HIV-1 transcription activation. Viruses 16, 116. doi: 10.3390/v16010116, PMID: 38257816
Randolph K. Hyder U. D’Orso I. (2022). KAP1/TRIM28: transcriptional activator and/or repressor of viral and cellular programs? Front. Cell. Infect. Microbiol. 12. doi: 10.3389/fcimb.2022.834636, PMID: 35281453
Rapone R. Del Maestro L. Bouyioukos C. Albini S. Cruz-Tapias P. Joliot V. et al. (2023). The cytoplasmic fraction of the histone lysine methyltransferase Setdb1 is essential for embryonic stem cells. iScience 26, 107386. doi: 10.1016/j.isci.2023.107386, PMID: 37559904
Rauwel B. Jang S. M. Cassano M. Kapopoulou A. Barde I. Trono D. (2015). Release of human cytomegalovirus from latency by a KAP1/TRIM28 phosphorylation switch. eLife 4, e06068. doi: 10.7554/eLife.06068, PMID: 25846574
Reichel A. Stilp A.-C. Scherer M. Reuter N. Lukassen S. Kasmapour B. et al. (2018). Chromatin-remodeling factor SPOC1 acts as a cellular restriction factor against human cytomegalovirus by repressing the major immediate early promoter. J. Virol. 92, e00342–e00318. doi: 10.1128/JVI.00342-18, PMID: 29743358
Ren J. Wang S. Zong Z. Pan T. Liu S. Mao W. et al. (2024). TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence. Nat. Commun. 15, 244. doi: 10.1038/s41467-023-44502-6, PMID: 38172120
Robbez-Masson L. Tie C. H. C. Conde L. Tunbak H. Husovsky C. Tchasovnikarova I. A. et al. (2018). The HUSH complex cooperates with TRIM28 to repress young retrotransposons and new genes. Genome Res. 28, 836–845. doi: 10.1101/gr.228171.117, PMID: 29728366
Rosspopoff O. Trono D. (2023). Take a walk on the KRAB side. Trends Genet. 39, 844–857. doi: 10.1016/j.tig.2023.08.003, PMID: 37716846
Rowe H. M. Jakobsson J. Mesnard D. Rougemont J. Reynard S. Aktas T. et al. (2010). KAP1 controls endogenous retroviruses in embryonic stem cells. Nature 463, 237–240. doi: 10.1038/nature08674, PMID: 20075919
Rozman B. Nachshon A. Levi Samia R. Lavi M. Schwartz M. Stern-Ginossar N. (2022). Temporal dynamics of HCMV gene expression in lytic and latent infections. Cell Rep. 39, 110653. doi: 10.1016/j.celrep.2022.110653, PMID: 35417700
Sahu R. K. Dhakshnamoorthy J. Jain S. Folco H. D. Wheeler D. Grewal S. I. S. (2024). Nucleosome remodeler exclusion by histone deacetylation enforces heterochromatic silencing and epigenetic inheritance. Mol. Cell 84, 3175–3191.e8. doi: 10.1016/j.molcel.2024.07.006, PMID: 39096900
Sakai M. Masuda Y. Tarumoto Y. Aihara N. Tsunoda Y. Iwata M. et al. (2024). Genome-scale CRISPR-Cas9 screen identifies host factors as potential therapeutic targets for SARS-CoV-2 infection. iScience 27, 110475. doi: 10.1016/j.isci.2024.110475, PMID: 39100693
Sales-Gil R. Vagnarelli P. (2020). How HP1 post-translational modifications regulate heterochromatin formation and maintenance. Cells 9, 1460. doi: 10.3390/cells9061460, PMID: 32545538
Sampath Kumar A. Seah M. K. Y. Ling K. Y. Wang Y. Tan J. H. L. Nitsch S. et al. (2017). Loss of maternal Trim28 causes male-predominant early embryonic lethality. Genes Dev. 31, 12–17. doi: 10.1101/gad.291195.116, PMID: 28115466
Santoni De Sio F. R. (2014). Kruppel-associated box (KRAB) proteins in the adaptive immune system. Nucleus 5, 138–148. doi: 10.4161/nucl.28738, PMID: 24699165
Santoni De Sio F. R. Massacand J. Barde I. Offner S. Corsinotti A. Kapopoulou A. et al. (2012). KAP1 regulates gene networks controlling mouse B-lymphoid cell differentiation and function. Blood 119, 4675–4685. doi: 10.1182/blood-2011-12-401117, PMID: 22452978
Santos J. Gil J. (2014). TRIM28/KAP1 regulates senescence. Immunol. Lett. 162, 281–289. doi: 10.1016/j.imlet.2014.08.011, PMID: 25160591
Schichl K. Doorbar J. (2025). Regulation and deregulation of viral gene expression during high-risk HPV infection. Viruses 17, 937. doi: 10.3390/v17070937, PMID: 40733555
Schmidt N. Domingues P. Golebiowski F. Patzina C. Tatham M. H. Hay R. T. et al. (2019). An influenza virus-triggered SUMO switch orchestrates co-opted endogenous retroviruses to stimulate host antiviral immunity. Proc. Natl. Acad. Sci. U.S.A. 116, 17399–17408. doi: 10.1073/pnas.1907031116, PMID: 31391303
Schneeberger P. E. Bierhals T. Neu A. Hempel M. Kutsche K. (2019). de novo MEPCE nonsense variant associated with a neurodevelopmental disorder causes disintegration of 7SK snRNP and enhanced RNA polymerase II activation. Sci. Rep. 9, 12516. doi: 10.1038/s41598-019-49032-0, PMID: 31467394
Schoelz J. M. Riddle N. C. (2022). Functions of HP1 proteins in transcriptional regulation. Epigenet. Chromatin 15, 14. doi: 10.1186/s13072-022-00453-8, PMID: 35526078
Schultz D. C. Ayyanathan K. Negorev D. Maul G. G. Rauscher F. J. (2002). SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 16, 919–932. doi: 10.1101/gad.973302, PMID: 11959841
Shah P. A. Boutros-Suleiman S. Emanuelli A. Paolini B. Levy-Cohen G. Blank M. (2022). The emerging role of E3 ubiquitin ligase SMURF2 in the regulation of transcriptional co-repressor KAP1 in untransformed and cancer cells and tissues. Cancers 14, 1607. doi: 10.3390/cancers14071607, PMID: 35406379
Sharma A. L. Tyagi P. Khumallambam M. Tyagi M. (2024). Cocaine-induced DNA-dependent protein kinase relieves RNAP II pausing by promoting TRIM28 phosphorylation and RNAP II hyperphosphorylation to enhance HIV transcription. Cells 13, 1950. doi: 10.3390/cells13231950, PMID: 39682697
Siebels S. Czech-Sioli M. Spohn M. Schmidt C. Theiss J. Indenbirken D. et al. (2020). Merkel cell polyomavirus DNA replication induces senescence in human dermal fibroblasts in a kap1/trim28-dependent manner. mBio 11, e00142–e00120. doi: 10.1128/mBio.00142-20, PMID: 32156811
Sio F. R. S. Barde I. Offner S. Kapopoulou A. Corsinotti A. Bojkowska K. et al. (2012). KAP1 regulates gene networks controlling T-cell development and responsiveness. FASEB J. 26, 4561–4575. doi: 10.1096/fj.12-206177, PMID: 22872677
Soldan S. S. Lieberman P. M. (2023). Epstein–Barr virus and multiple sclerosis. Nat. Rev. Microbiol. 21, 51–64. doi: 10.1038/s41579-022-00770-5, PMID: 35931816
Spearman C. W. Dusheiko G. M. Hellard M. Sonderup M. (2019). Hepatitis C. Lancet 394, 1451–1466. doi: 10.1016/S0140-6736(19)32320-7, PMID: 31631857
Sripathy S. P. Stevens J. Schultz D. C. (2006). The KAP1 corepressor functions to coordinate the assembly of de novo HP1-demarcated microenvironments of heterochromatin required for KRAB zinc finger protein-mediated transcriptional repression. Mol. Cell. Biol. 26, 8623–8638. doi: 10.1128/MCB.00487-06, PMID: 16954381
Steiner S. Kratzel A. Barut G. T. Lang R. M. Aguiar Moreira E. Thomann L. et al. (2024). SARS-CoV-2 biology and host interactions. Nat. Rev. Microbiol. 22, 206–225. doi: 10.1038/s41579-023-01003-z, PMID: 38225365
Stoll G. A. Oda S. Chong Z.-S. Yu M. McLaughlin S. H. Modis Y. (2019). Structure of KAP1 tripartite motif identifies molecular interfaces required for retroelement silencing. Proc. Natl. Acad. Sci. U.S.A. 116, 15042–15051. doi: 10.1073/pnas.1901318116, PMID: 31289231
Stoll G. A. Pandiloski N. Douse C. H. Modis Y. (2022). Structure and functional mapping of the KRAB-KAP1 repressor complex. EMBO J. 41, e111179. doi: 10.15252/embj.2022111179, PMID: 36341546
Sun Y. Keown J. R. Black M. M. Raclot C. Demarais N. Trono D. et al. (2019). A dissection of oligomerization by the TRIM28 tripartite motif and the interaction with members of the krab-ZFP family. J. Mol. Biol. 431, 2511–2527. doi: 10.1016/j.jmb.2019.05.002, PMID: 31078555
Sun R. Liang D. Gao Y. Lan K. (2014). Kaposi’s sarcoma-associated herpesvirus-encoded LANA interacts with host KAP1 to facilitate establishment of viral latency. J. Virol. 88, 7331–7344. doi: 10.1128/JVI.00596-14, PMID: 24741090
Swinkels H. M. Nguyen A. D. Gulick P. G. (2025). “HIV and AIDS,” in StatPearls (StatPearls Publishing, Treasure Island (FL). Available online at: http://www.ncbi.nlm.nih.gov/books/NBK534860/.
Taka J. R. H. Sun Y. Goldstone D. C. (2022). Mapping the interaction between Trim28 and the KRAB domain at the center of Trim28 silencing of endogenous retroviruses. Protein Sci. 31, e4436. doi: 10.1002/pro.4436, PMID: 36173157
Tan J. Sun X. Zhao H. Guan H. Gao S. Zhou P. (2023). Double-strand DNA break repair: molecular mechanisms and therapeutic targets. MedComm 4, e388. doi: 10.1002/mco2.388, PMID: 37808268
Tanaka S. Pfleger C. Lai J.-F. Roan F. Sun S.-C. Ziegler S. F. (2018). KAP1 regulates regulatory T cell function and proliferation in both foxp3-dependent and -independent manners. Cell Rep. 23, 796–807. doi: 10.1016/j.celrep.2018.03.099, PMID: 29669285
Taura M. Song E. Ho Y.-C. Iwasaki A. (2019). Apobec3A maintains HIV-1 latency through recruitment of epigenetic silencing machinery to the long terminal repeat. Proc. Natl. Acad. Sci. U.S.A. 116, 2282–2289. doi: 10.1073/pnas.1819386116, PMID: 30670656
Tavakoli R. Rahimi P. Hamidi-Fard M. Eybpoosh S. Doroud D. Ahmadi I. et al. (2022). Comparing the expression levels of tripartite motif containing 28 in mild and severe COVID-19 infection. Virol. J. 19, 156. doi: 10.1186/s12985-022-01885-0, PMID: 36192760
Thierry E. Brennich M. Round A. Buisson M. Burmeister W. P. Hutin S. (2015). Production and characterisation of Epstein–Barr virus helicase–primase complex and its accessory protein BBLF2/3. Virus Genes 51, 171–181. doi: 10.1007/s11262-015-1233-6, PMID: 26292944
Thiru A. Nietlispach D. Mott H. R. Okuwaki M. Lyon D. Nielsen P. R. et al. (2004). Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin. EMBO J. 23, 489–499. doi: 10.1038/sj.emboj.7600088, PMID: 14765118
Tie C. H. Fernandes L. Conde L. Robbez-Masson L. Sumner R. P. Peacock T. et al. (2018). KAP 1 regulates endogenous retroviruses in adult human cells and contributes to innate immune control. EMBO Rep. 19, e45000. doi: 10.15252/embr.201745000, PMID: 30061100
Tovo P.-A. Davico C. Marcotulli D. Vitiello B. Daprà V. Calvi C. et al. (2022). Enhanced expression of human endogenous retroviruses, TRIM28 and SETDB1 in autism spectrum disorder. IJMS 23, 5964. doi: 10.3390/ijms23115964, PMID: 35682642
Tovo P.-A. Galliano I. Parodi E. Calvi C. Gambarino S. Licciardi F. et al. (2023a). Children with chronic immune thrombocytopenia exhibit high expression of human endogenous retroviruses TRIM28 and SETDB1. Genes 14, 1569. doi: 10.3390/genes14081569, PMID: 37628621
Tovo P.-A. Garazzino S. Daprà V. Alliaudi C. Silvestro E. Calvi C. et al. (2020a). Chronic HCV infection is associated with overexpression of human endogenous retroviruses that persists after drug-induced viral clearance. IJMS 21, 3980. doi: 10.3390/ijms21113980, PMID: 32492928
Tovo P.-A. Garazzino S. Daprà V. Pruccoli G. Calvi C. Mignone F. et al. (2021). COVID-19 in children: expressions of type I/II/III interferons, TRIM28, SETDB1, and endogenous retroviruses in mild and severe cases. IJMS 22, 7481. doi: 10.3390/ijms22147481, PMID: 34299101
Tovo P.-A. Garazzino S. Savino F. Daprà V. Pruccoli G. Dini M. et al. (2023b). Expressions of type I and III interferons, endogenous retroviruses, TRIM28, and SETDB1 in children with respiratory syncytial virus bronchiolitis. CIMB 45, 1197–1217. doi: 10.3390/cimb45020079, PMID: 36826024
Tovo P.-A. Marozio L. Abbona G. Calvi C. Frezet F. Gambarino S. et al. (2023c). Pregnancy is associated with impaired transcription of human endogenous retroviruses and of TRIM28 and SETDB1, particularly in mothers affected by multiple sclerosis. Viruses 15, 710. doi: 10.3390/v15030710, PMID: 36992419
Tovo P.-A. Rabbone I. Tinti D. Galliano I. Trada M. Daprà V. et al. (2020b). Enhanced expression of human endogenous retroviruses in new-onset type 1 diabetes: Potential pathogenetic and therapeutic implications. Autoimmunity 53, 283–288. doi: 10.1080/08916934.2020.1777281, PMID: 32586158
Turelli P. Castro-Diaz N. Marzetta F. Kapopoulou A. Raclot C. Duc J. et al. (2014). Interplay of TRIM28 and DNA methylation in controlling human endogenous retroelements. Genome Res. 24, 1260–1270. doi: 10.1101/gr.172833.114, PMID: 24879559
V’kovski P. Kratzel A. Steiner S. Stalder H. Thiel V. (2021). Coronavirus biology and replication: implications for SARS-CoV-2. Nat. Rev. Microbiol. 19, 155–170. doi: 10.1038/s41579-020-00468-6, PMID: 33116300
Venturini L. You J. Stadler M. Galien R. Lallemand V. Koken M. H. et al. (1999). TIF1γ, a novel member of the transcriptional intermediary factor 1 family. Oncogene 18, 1209–1217. doi: 10.1038/sj.onc.1202655, PMID: 10022127
Vianelli N. Auteri G. Buccisano F. Carrai V. Baldacci E. Clissa C. et al. (2022). Refractory primary immune thrombocytopenia (ITP): current clinical challenges and therapeutic perspectives. Ann. Hematol. 101, 963–978. doi: 10.1007/s00277-022-04786-y, PMID: 35201417
Volkmann E. R. Andréasson K. Smith V. (2023). Systemic sclerosis. Lancet 401, 304–318. doi: 10.1016/S0140-6736(22)01692-0, PMID: 36442487
Wang Y. Du S. Zhu C. Wang C. Yu N. Lin Z. et al. (2020a). STUB1 is targeted by the SUMO-interacting motif of EBNA1 to maintain Epstein-Barr Virus latency. PloS Pathog. 16, e1008447. doi: 10.1371/journal.ppat.1008447, PMID: 32176739
Wang Y. Fan Y. Huang Y. Du T. Liu Z. Huang D. et al. (2021). TRIM28 regulates SARS-CoV-2 cell entry by targeting ACE2. Cell. Signalling 85, 110064. doi: 10.1016/j.cellsig.2021.110064, PMID: 34146659
Wang L. Gao Y. Zheng X. Liu C. Dong S. Li R. et al. (2019). Histone modifications regulate chromatin compartmentalization by contributing to a phase separation mechanism. Mol. Cell 76, 646–659.e6. doi: 10.1016/j.molcel.2019.08.019, PMID: 31543422
Wang C. Goff S. P. (2017). Differential control of retrovirus silencing in embryonic cells by proteasomal regulation of the ZFP809 retroviral repressor. Proc. Natl. Acad. Sci. U.S.A. 114, E922–E930. doi: 10.1073/pnas.1620879114, PMID: 28115710
Wang C. Ivanov A. Chen L. Fredericks W. J. Seto E. Rauscher F. J. et al. (2005). MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation. EMBO J. 24, 3279–3290. doi: 10.1038/sj.emboj.7600791, PMID: 16107876
Wang X. Li Y. Shi T. Bont L. J. Chu H. Y. Zar H. J. et al. (2024). Global disease burden of and risk factors for acute lower respiratory infections caused by respiratory syncytial virus in preterm infants and young children in 2019: a systematic review and meta-analysis of aggregated and individual participant data. Lancet 403, 1241–1253. doi: 10.1016/S0140-6736(24)00138-7, PMID: 38367641
Wang Y. Singh A. R. Zhao Y. Du T. Huang Y. Wan X. et al. (2020b). TRIM28 regulates sprouting angiogenesis through VEGFR-DLL4-Notch signaling circuit. FASEB J. 34, 14710–14724. doi: 10.1096/fj.202000186RRR, PMID: 32918765
Wang G. Z. Wolf D. Goff S. P. (2014). EBP1, a novel host factor involved in primer binding site-dependent restriction of moloney murine leukemia virus in embryonic cells. J. Virol. 88, 1825–1829. doi: 10.1128/JVI.02578-13, PMID: 24227866
Weber P. Cammas F. Gerard C. Metzger D. Chambon P. Losson R. et al. (2002). Germ cell expression of the transcriptional co-repressor TIF1β is required for the maintenance of spermatogenesis in the mouse. Development 129, 2329–2337. doi: 10.1242/dev.129.10.2329, PMID: 11973266
Weber M. Padmanabhan Nair V. Bauer T. Sprinzl M. F. Protzer U. Vincendeau M. (2021). Increased HERV-K(HML-2) transcript levels correlate with clinical parameters of liver damage in hepatitis C patients. Cells 10, 774. doi: 10.3390/cells10040774, PMID: 33807462
Wei J. Sun Y. Wang T. Zhu G. Liu W. He X. et al. (2022). The regulation of prototype foamy virus 5′Long terminal repeats and internal promoter by endogenous transcription factors. Intervirology 65, 17–28. doi: 10.1159/000517539, PMID: 34438397
White D. E. Negorev D. Peng H. Ivanov A. V. Maul G. G. Rauscher F. J. (2006). KAP1, a novel substrate for PIKK family members, colocalizes with numerous damage response factors at DNA lesions. Cancer Res. 66, 11594–11599. doi: 10.1158/0008-5472.CAN-06-4138, PMID: 17178852
White D. Rafalska-Metcalf I. U. Ivanov A. V. Corsinotti A. Peng H. Lee S.-C. et al. (2012). The ATM substrate KAP1 controls DNA repair in heterochromatin: regulation by HP1 proteins and serine 473/824 phosphorylation. Mol. Cancer Res. 10, 401–414. doi: 10.1158/1541-7786.MCR-11-0134, PMID: 22205726
Wildenbeest J. G. Lowe D. M. Standing J. F. Butler C. C. (2024). Respiratory syncytial virus infections in adults: a narrative review. Lancet Respir. Med. 12, 822–836. doi: 10.1016/S2213-2600(24)00255-8, PMID: 39265602
Wolf D. Cammas F. Losson R. Goff S. P. (2008). Primer binding site-dependent restriction of murine leukemia virus requires HP1 binding by TRIM28. J. Virol. 82, 4675–4679. doi: 10.1128/JVI.02445-07, PMID: 18287239
Wolf D. Goff S. P. (2007). TRIM28 mediates primer binding site-targeted silencing of murine leukemia virus in embryonic cells. Cell 131, 46–57. doi: 10.1016/j.cell.2007.07.026, PMID: 17923087
Xiao X. Fu Y. You W. Huang C. Zeng F. Gu X. et al. (2024). Inhibition of the RLR signaling pathway by SARS-CoV-2 ORF7b is mediated by MAVS and abrogated by ORF7b-homologous interfering peptide. J. Virol. 98, e01573–e01523. doi: 10.1128/jvi.01573-23, PMID: 38572974
Xu H. Akinyemi I. A. Haley J. McIntosh M. T. Bhaduri-McIntosh S. (2023). ATM, KAP1 and the Epstein–Barr virus polymerase processivity factor direct traffic at the intersection of transcription and replication. Nucleic Acids Res. 51, 11104–11122. doi: 10.1093/nar/gkad823, PMID: 37852757
Xu S. Jin T. Weng J. (2022b). Endothelial cells as a key cell type for innate immunity: A focused review on RIG-I signaling pathway. Front. Immunol. 13. doi: 10.3389/fimmu.2022.951614, PMID: 35865527
Xu H. Li X. Rousseau B. A. Akinyemi I. A. Frey T. R. Zhou K. et al. (2022a). IFI16 partners with KAP1 to maintain epstein-barr virus latency. J. Virol. 96, e01028–e01022. doi: 10.1128/jvi.01028-22, PMID: 35969079
Xue C. Meng H. Niu W. Li M. Wei J. Chen S. et al. (2024). TRIM28 promotes tumor growth and metastasis in breast cancer by targeting the BRD7 protein for ubiquitination and degradation. Cell Oncol. 47, 1973–1993. doi: 10.1007/s13402-024-00981-3, PMID: 39222175
Yamauchi M. Freitag B. Khan C. Berwin B. Barklis E. (1995). Stem cell factor binding to retrovirus primer binding site silencers. J. Virol. 69, 1142–1149. doi: 10.1128/jvi.69.2.1142-1149.1995, PMID: 7529329
Yan Q. Zhou J. Gu Y. Huang W. Ruan M. Zhang H. et al. (2024). Lactylation of NAT10 promotes N4-acetylcytidine modification on tRNASer-CGA-1–1 to boost oncogenic DNA virus KSHV reactivation. Cell Death Differ 31, 1362–1374. doi: 10.1038/s41418-024-01327-0, PMID: 38879723
Yang B. X. El Farran C. A. Guo H. C. Yu T. Fang H. T. Wang H. F. et al. (2015). Systematic identification of factors for provirus silencing in embryonic stem cells. Cell 163, 230–245. doi: 10.1016/j.cell.2015.08.037, PMID: 26365490
Yang D. Geng T. Harrison A. G. Cahoon J. G. Xing J. Jiao B. et al. (2024). UBR5 promotes antiviral immunity by disengaging the transcriptional brake on RIG-I like receptors. Nat. Commun. 15, 780. doi: 10.1038/s41467-024-45141-1, PMID: 38278841
Yang F. Tanasa B. Micheletti R. Ohgi K. A. Aggarwal A. K. Rosenfeld M. G. (2021). Shape of promoter antisense RNAs regulates ligand-induced transcription activation. Nature 595, 444–449. doi: 10.1038/s41586-021-03589-x, PMID: 34194047
Yang Y. Wang T. Fu Y. Li X. Yu F. (2025). TRIM28 functions as SUMO ligase to SUMOylate TRAF6 and regulate NF-κB activation in HBV-replicating cells. Hepatol. Int 19, 529–546. doi: 10.1007/s12072-025-10779-6, PMID: 39920527
Yoneyama M. Kato H. Fujita T. (2024). Physiological functions of RIG-I-like receptors. Immunity 57, 731–751. doi: 10.1016/j.immuni.2024.03.003, PMID: 38599168
Yuan P. Yan J. Wang S. Guo Y. Xi X. Han S. et al. (2021). Trim28 acts as restriction factor of prototype foamy virus replication by modulating H3K9me3 marks and destabilizing the viral transactivator Tas. Retrovirology 18, 38. doi: 10.1186/s12977-021-00584-y, PMID: 34903241
Zeng L. Yap K. L. Ivanov A. V. Wang X. Mujtaba S. Plotnikova O. et al. (2008). Structural insights into human KAP1 PHD finger–bromodomain and its role in gene silencing. Nat. Struct. Mol. Biol. 15, 626–633. doi: 10.1038/nsmb.1416, PMID: 18488044
Zhai Y. Zhang M. An X. Zhang S. Kong X. Li Q. et al. (2021). TRIM28 maintains genome imprints and regulates development of porcine SCNT embryos. Reproduction 161, 411–424. doi: 10.1530/REP-20-0602, PMID: 33539314
Zhang Y. Wan X. Qiu L. Zhou L. Huang Q. Wei M. et al. (2023b). Trim28 citrullination maintains mouse embryonic stem cell pluripotency via regulating Nanog and Klf4 transcription. Sci. China Life Sci. 66, 545–562. doi: 10.1007/s11427-022-2167-3, PMID: 36100837
Zhang F.-L. Yang S.-Y. Liao L. Zhang T.-M. Zhang Y.-L. Hu S.-Y. et al. (2023a). Dynamic SUMOylation of MORC2 orchestrates chromatin remodelling and DNA repair in response to DNA damage and drives chemoresistance in breast cancer. Theranostics 13, 973–990. doi: 10.7150/thno.79688, PMID: 36793866
Zhang H. Zheng H. Zhu J. Dong Q. Wang J. Fan H. et al. (2021). Ubiquitin-modified proteome of SARS-coV-2-infected host cells reveals insights into virus–host interaction and pathogenesis. J. Proteome Res. 20, 2224–2239. doi: 10.1021/acs.jproteome.0c00758, PMID: 33666082
Zhang L. Zhu C. Guo Y. Wei F. Lu J. Qin J. et al. (2014). Inhibition of KAP1 enhances hypoxia-induced kaposi’s sarcoma-associated herpesvirus reactivation through RBP-Jκ. J. Virol. 88, 6873–6884. doi: 10.1128/JVI.00283-14, PMID: 24696491
Zhao X. (2018). SUMO-mediated regulation of nuclear functions and signaling processes. Mol. Cell 71, 409–418. doi: 10.1016/j.molcel.2018.07.027, PMID: 30075142
Zhao Y. Gao Y. Guyatt G. Uyeki T. M. Liu P. Liu M. et al. (2024). Antivirals for post-exposure prophylaxis of influenza: a systematic review and network meta-analysis. Lancet 404, 764–772. doi: 10.1016/S0140-6736(24)01357-6, PMID: 39181596
Zheng L. Pan H. Li S. Flesken-Nikitin A. Chen P.-L. Boyer T. G. et al. (2000). Sequence-specific transcriptional corepressor function for BRCA1 through a novel zinc finger protein, ZBRK1. Mol. Cell 6, 757–768. doi: 10.1016/S1097-2765(00)00075-7, PMID: 11090615
Zhu X. Li F. Fan B. Zhao Y. Zhou J. Wang D. et al. (2024). TRIM28 regulates the coagulation cascade inhibited by p72 of African swine fever virus. Vet. Res. 55, 149. doi: 10.1186/s13567-024-01407-6, PMID: 39533356
Zhu Q. Xiao Y. (2024). “The immune modulatory role of TIF1 proteins,” in Ubiquitination in Immune System and Immune Response. Eds. Hu H. Fu X. (Springer Nature Singapore, Singapore), 89–99. doi: 10.1007/978-981-97-7288-9_6, PMID: 39546137
Ziegler V. Deußen M. Schumacher L. Roos W. P. Fritz G. (2020). Anticancer drug and ionizing radiation-induced DNA damage differently influences transcription activity and DDR-related stress responses of an endothelial monolayer. Biochim. Biophys. Acta (BBA) - Mol. Cell Res. 1867, 118678. doi: 10.1016/j.bbamcr.2020.118678, PMID: 32061892