去泛素化酶OTUs的功能及在人类疾病中的研究进展
南京医科大学第二附属医院, 儿科, 江苏南京 211100
| 摘 要： | 卵巢肿瘤相关蛋白酶（ovarian tumor domain proteases, OTUs），这一独特的蛋白酶家族，包含着四个各具特色的亚家族，它们在生物体内扮演着至关重要的角色。作为去泛素化酶这一庞大酶类家族中的核心成员，OTUs通过精确调控蛋白质的泛素化水平，广泛参与到细胞分裂、免疫反应和凋亡等一系列复杂而精细的生理过程中，发挥着不可或缺的调节功能。近年来，随着研究的不断深入，越来越多的证据表明，这些生理过程的失调与人类多种疾病的发生和发展密切相关。无论是非感染性疾病，如肿瘤、肾脏疾病、自身免疫性疾病和神经退行性疾病，还是感染性疾病，如病毒、细菌和寄生虫感染，都可能与OTUs的功能异常有关。因此，对OTUs的功能及其在人类疾病中的关系进行深入的研究和综述，不仅有助于我们更好地理解这些疾病的发病机制，还为研究和利用去泛素化酶OTUs治疗疾病提供了新的思路和方向。通过揭示OTUs在疾病中的作用机制，我们可以开发出针对特定疾病的治疗策略，如通过抑制或激活特定的OTUs成员，来调节相关疾病的病理过程，从而达到治疗的目的。同时，对OTUs的研究也有助于我们发现新的药物靶点，为药物研发提供新的思路和方法。本文通过对OTUs的功能以及在人类疾病中的关系作一回顾及综述，以期为研究和利用去泛素化酶OTUs治疗疾病提供参考。 |
| 关 键 词： | 去泛素化酶; OTUs; 非感染性疾病; 感染性疾病 |
| DOI： | 10.57237/j.mrf.2024.04.001 |
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收稿日期: 2024-09-20
接受日期: 2024-12-03
在线出版日期: 2024-12-23
The Function of OTUs and Research Progress in Human Diseases
Pediatric Department, The Second Affiliated Hospital of Nanjing Medical University, Nanjing 211100, China
| Abstract: | Ovarian tumor domain proteases (OTUs), a unique protease family, contains four distinctive subfamilies, which play crucial roles in organisms. As a core member of the large enzyme family of deubiquitinases, OTUs play an indispensable regulatory role in a series of complex and delicate physiological processes such as cell division, immune response and apoptosis by precisely regulating the ubiquitination level of proteins. In recent years, with the deepening of research, more and more evidence shows that the dysregulation of these physiological processes is closely related to the occurrence and development of a variety of human diseases. Whether non infectious diseases, such as tumors, kidney diseases, autoimmune diseases and neurodegenerative diseases, or infectious diseases, such as viral, bacterial and parasitic infections, may be related to the dysfunction of OTUs. Therefore, an in-depth study and review of the functions of OTUs and their relationship in human diseases will not only help us better understand the pathogenesis of these diseases, but also provide new ideas and directions for the research and use of deubiquitinase OTUs in the treatment of diseases. By revealing the mechanism of OTUs in diseases, we can develop therapeutic strategies for specific diseases, such as regulating the pathological process of related diseases by inhibiting or activating specific OTUs members, so as to achieve the purpose of treatment. At the same time, the study of OTUs also helps us find new drug targets and provides new ideas and methods for drug research and development. This article reviews the functions of OTUs and their relationship in human diseases, in order to provide references for the research and use of deubiquitinase OTUs in the treatment of diseases. |
| Keywords: | Deubiquitination Enzymes; OTUs; Noninfectious Diseases; Infectious Diseases |
基金
| 1. | 江苏省自然科学基金 (BK20210982) |
| 2. | 国家自然科学基金 (82100719) |
参考文献
| [1] | Pla-Prats, C. and N. H. Thomä (2022) Quality control of protein complex assembly by the ubiquitin-proteasome system Trends In Cell Biology. 32(8): 696-706. https://doi.org/10.1016/j.tcb.2022.02.005 |
| [2] | Tran, H., et al. (2008) Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains Genes & Development. 22(4): 528-542. https://doi.org/10.1101/gad.463208 |
| [3] | Lange, S. M., L. A. Armstrong, and Y. Kulathu (2022) Deubiquitinases: From mechanisms to their inhibition by small molecules Molecular Cell. 82(1): 15-29. https://doi.org/10.1016/j.molcel.2021.10.027 |
| [4] | Bonacci, T. and M. J. Emanuele (2020) Dissenting degradation: Deubiquitinases in cell cycle and cancer Seminars In Cancer Biology. 67(Pt 2): 145-158. https://doi.org/10.1016/j.semcancer.2020.03.008 |
| [5] | Du, J., et al. (2020) The function and regulation of OTU deubiquitinases Frontiers of Medicine. 14(5): 542-563. https://doi.org/10.1007/s11684-019-0734-4 |
| [6] | Mevissen, T. E. T., et al. (2013) OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis Cell. 154(1): 169-184. https://doi.org/10.1016/j.cell.2013.05.046 |
| [7] | Zhu, Q., et al. (2021) The functions and regulation of Otubains in protein homeostasis and diseases Ageing Research Reviews. 67: 101303. https://doi.org/10.1016/j.arr.2021.101303 |
| [8] | Mevissen, T. E. T. and D. Komander (2017) Mechanisms of Deubiquitinase Specificity and Regulation Annual Review of Biochemistry. 86: 159-192. https://doi.org/10.1146/annurev-biochem-061516-044916 |
| [9] | Suresh, H. G., N. Pascoe, and B. Andrews (2020) The structure and function of deubiquitinases: lessons from budding yeast Open Biology. 10(10): 200279. https://doi.org/10.1098/rsob.200279 |
| [10] | Wiener, R., et al. (2012) The mechanism of OTUB1-mediated inhibition of ubiquitination Nature. 483(7391): 618-622. https://doi.org/10.1038/nature10911 |
| [11] | Bailey-Elkin, B. A., et al. (2017) Structure and Function of Viral Deubiquitinating Enzymes Journal of Molecular Biology. 429(22): 3441-3470. https://doi.org/10.1016/j.jmb.2017.06.010 |
| [12] | Li, Y. and D. Reverter (2021) Molecular Mechanisms of DUBs Regulation in Signaling and Disease International Journal of Molecular Sciences. 22(3). https://doi.org/10.3390/ijms22030986 |
| [13] | Mulas, F., et al. (2021) The deubiquitinase OTUB1 augments NF-κB-dependent immune responses in dendritic cells in infection and inflammation by stabilizing UBC13 Cellular & Molecular Immunology. 18(6): 1512-1527. https://doi.org/10.1038/s41423-020-0362-6 |
| [14] | Liao, Y., et al. (2022) Deubiquitinating enzyme OTUB1 in immunity and cancer: Good player or bad actor? Cancer Letters. 526: 248-258. https://doi.org/10.1016/j.canlet.2021.12.002 |
| [15] | Nakada, S., et al. (2010) Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1 Nature. 466(7309): 941-946. https://doi.org/10.1038/nature09297 |
| [16] | Liu, T., et al. (2019) The Deubiquitylase OTUB1 Mediates Ferroptosis via Stabilization of SLC7A11 Cancer Research. 79(8): 1913-1924. https://doi.org/10.1158/0008-5472.CAN-18-3037 |
| [17] | Altun, M., et al. (2015) The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages PloS One. 10(1): e0115344. https://doi.org/10.1371/journal.pone.0115344 |
| [18] | Qian, M., et al. (2021) Deubiquitinase JOSD2 stabilizes YAP/TAZ to promote cholangiocarcinoma progression Acta Pharmaceutica Sinica. B. 11(12): 4008-4019. https://doi.org/10.1016/j.apsb.2021.04.003 |
| [19] | Li, J., et al. (2019) OTUB2 stabilizes U2AF2 to promote the Warburg effect and tumorigenesis via the AKT/mTOR signaling pathway in non-small cell lung cancer Theranostics. 9(1): 179-195. https://doi.org/10.7150/thno.29545 |
| [20] | Yu, S., et al. (2022) Deubiquitinase OTUB2 exacerbates the progression of colorectal cancer by promoting PKM2 activity and glycolysis Oncogene. 41(1): 46-56. https://doi.org/10.1038/s41388-021-02071-2 |
| [21] | Kato, K., et al. (2014) Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice Molecular Cell. 53(4): 617-630. https://doi.org/10.1016/j.molcel.2014.01.030 |
| [22] | Wu, B., et al. (2022) The deubiquitinase OTUD1 inhibits colonic inflammation by suppressing RIPK1-mediated NF-κB signaling Cellular & Molecular Immunology. 19(2): 276-289. https://doi.org/10.1038/s41423-021-00810-9 |
| [23] | Chen, X., et al. (2021) OTUD1 Regulates Antifungal Innate Immunity through Deubiquitination of CARD9 Journal of Immunology (Baltimore, Md.: 1950). 206(8): 1832-1843. https://doi.org/10.4049/jimmunol.2001253 |
| [24] | Zhang, Z., et al. (2020) OTUD1 Negatively Regulates Type I IFN Induction by Disrupting Noncanonical Ubiquitination of IRF3 Journal of Immunology (Baltimore, Md.: 1950). 204(7): 1904-1918. https://doi.org/10.4049/jimmunol.1900305 |
| [25] | Zhang, L., et al. (2018) Induction of OTUD1 by RNA viruses potently inhibits innate immune responses by promoting degradation of the MAVS/TRAF3/TRAF6 signalosome PLoS Pathogens. 14(5): e1007067. https://doi.org/10.1371/journal.ppat.1007067 |
| [26] | Luo, Q., et al. (2021) OTUD1 Activates Caspase-Independent and Caspase-Dependent Apoptosis by Promoting AIF Nuclear Translocation and MCL1 Degradation Advanced Science (Weinheim, Baden-Wurttemberg, Germany). 8(8): 2002874. https://doi.org/10.1002/advs.202002874 |
| [27] | Oikawa, D., et al. (2022) OTUD1 deubiquitinase regulates NF-κB- and KEAP1-mediated inflammatory responses and reactive oxygen species-associated cell death pathways Cell Death & Disease. 13(8): 694. https://doi.org/10.1038/s41419-022-05145-5 |
| [28] | Song, J., et al. (2021) The deubiquitinase OTUD1 enhances iron transport and potentiates host antitumor immunity EMBO Reports. 22(2): e51162. https://doi.org/10.15252/embr.202051162 |
| [29] | Schimmack, G., et al. (2017) YOD1/TRAF6 association balances p62-dependent IL-1 signaling to NF-κB ELife. 6. https://doi.org/10.7554/eLife.22416 |
| [30] | Papadopoulos, C., et al. (2017) VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy The EMBO Journal. 36(2): 135-150. https://doi.org/10.15252/embj.201695148 |
| [31] | Kim, Y., et al. (2017) Deubiquitinase YOD1 potentiates YAP/TAZ activities through enhancing ITCH stability Proceedings of the National Academy of Sciences of the United States of America. 114(18): 4691-4696. https://doi.org/10.1073/pnas.1620306114 |
| [32] | Zhou, X.-L., et al. (2018) Targeting YOD1 by RNA Interference Inhibits Proliferation and Migration of Human Oral Keratinocytes through Transforming Growth Factor-3 Signaling Pathway BioMed Research International. 2018: 6254308. https://doi.org/10.1155/2018/6254308 |
| [33] | Yuan, L., et al. (2015) Deubiquitylase OTUD3 regulates PTEN stability and suppresses tumorigenesis Nature Cell Biology. 17(9): 1169-1181. https://doi.org/10.1038/ncb3218 |
| [34] | Du, T., et al. (2019) The deubiquitylase OTUD3 stabilizes GRP78 and promotes lung tumorigenesis Nature Communications. 10(1): 2914. https://doi.org/10.1038/s41467-019-10824-7 |
| [35] | Zhang, Z., et al. (2020) Acetylation-Dependent Deubiquitinase OTUD3 Controls MAVS Activation in Innate Antiviral Immunity Molecular Cell. 79(2). https://doi.org/10.1016/j.molcel.2020.06.020 |
| [36] | Wang, M., et al. (2021) Nicotine-mediated OTUD3 downregulation inhibits VEGF-C mRNA decay to promote lymphatic metastasis of human esophageal cancer Nature Communications. 12(1): 7006. https://doi.org/10.1038/s41467-021-27348-8 |
| [37] | Jaynes, P. W., et al. (2020) OTUD4 enhances TGFβ signalling through regulation of the TGFβ receptor complex Scientific Reports. 10(1): 15725. https://doi.org/10.1038/s41598-020-72791-0 |
| [38] | Zhao, Y., et al. (2018) OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-Dependent Signaling Molecular Cell. 69(3). https://doi.org/10.1016/j.molcel.2018.01.009 |
| [39] | Liu, H., et al. (2020) OTUD4 alleviates hepatic ischemia-reperfusion injury by suppressing the K63-linked ubiquitination of TRAF6 Biochemical and Biophysical Research Communications. 523(4): 924-930. https://doi.org/10.1016/j.bbrc.2019.12.114 |
| [40] | Liuyu, T., et al. (2019) Induction of OTUD4 by viral infection promotes antiviral responses through deubiquitinating and stabilizing MAVS Cell Research. 29(1): 67-79. https://doi.org/10.1038/s41422-018-0107-6 |
| [41] | Das, R., et al. (2019) New roles for the de-ubiquitylating enzyme OTUD4 in an RNA-protein network and RNA granules Journal of Cell Science. 132(12). https://doi.org/10.1242/jcs.229252 |
| [42] | Guo, Y., et al. (2021) OTUD5 promotes innate antiviral and antitumor immunity through deubiquitinating and stabilizing STING Cellular & Molecular Immunology. 18(8): 1945-1955. https://doi.org/10.1038/s41423-020-00531-5 |
| [43] | Li, F., et al. (2019) The deubiquitinase OTUD5 regulates Ku80 stability and non-homologous end joining Cellular and Molecular Life Sciences: CMLS. 76(19): 3861-3873. https://doi.org/10.1007/s00018-019-03094-5 |
| [44] | Park, S.-Y., et al. (2015) Deubiquitinase OTUD5 mediates the sequential activation of PDCD5 and p53 in response to genotoxic stress Cancer Letters. 357(1): 419-427. https://doi.org/10.1016/j.canlet.2014.12.005 |
| [45] | de Vivo, A., et al. (2019) The OTUD5-UBR5 complex regulates FACT-mediated transcription at damaged chromatin Nucleic Acids Research. 47(2): 729-746. https://doi.org/10.1093/nar/gky1219 |
| [46] | Cho, J. H., et al. (2021) Deubiquitinase OTUD5 is a positive regulator of mTORC1 and mTORC2 signaling pathways Cell Death and Differentiation. 28(3): 900-914. https://doi.org/10.1038/s41418-020-00649-z |
| [47] | Zhang, Y., et al. (2021) OTUD5-mediated deubiquitination of YAP in macrophage promotes M2 phenotype polarization and favors triple-negative breast cancer progression Cancer Letters. 504: 104-115. https://doi.org/10.1016/j.canlet.2021.02.003 |
| [48] | Dinallo, V., et al. (2022) The Deubiquitinating Enzyme OTUD5 Sustains Inflammatory Cytokine Response in Inflammatory Bowel Disease Journal of Crohn's & Colitis. 16(1): 122-132. https://doi.org/10.1093/ecco-jcc/jjab121 |
| [49] | Li, X., et al. (2022) Mechanism of OTUD5 in non-small cell lung cancer cell proliferation, invasion, and migration Bosnian Journal of Basic Medical Sciences. https://doi.org/10.17305/bjbms.2022.7206 |
| [50] | Shi, L., et al. (2020) Deubiquitinase OTUD6A promotes proliferation of cancer cells via regulating Drp1 stability and mitochondrial fission Molecular Oncology. 14(12): 3169-3183. https://doi.org/10.1002/1878-0261.12825 |
| [51] | Kim, H. J. and J. Kim (2021) OTUD6A Is an Aurora Kinase A-Specific Deubiquitinase International Journal of Molecular Sciences. 22(4). https://doi.org/10.3390/ijms22041936 |
| [52] | Zhao, Y., et al. (2022) Deubiquitinase OTUD6A promotes breast cancer progression by increasing TopBP1 stability and rendering tumor cells resistant to DNA-damaging therapy Cell Death and Differentiation. https://doi.org/10.1038/s41418-022-01036-6 |
| [53] | Liu, X., et al. (2020) Deubiquitylase OTUD6B Governs pVHL Stability in an Enzyme-Independent Manner and Suppresses Hepatocellular Carcinoma Metastasis Advanced Science (Weinheim, Baden-Wurttemberg, Germany). 7(8): 1902040. https://doi.org/10.1002/advs.201902040 |
| [54] | Takata, M., et al. (2019) OTUD6B-AS1 Might Be a Novel Regulator of Apoptosis in Systemic Sclerosis Frontiers In Immunology. 10: 1100. https://doi.org/10.3389/fimmu.2019.01100 |
| [55] | Wang, Z., et al. (2020) OTUD6B-AS1 Inhibits Viability, Migration, and Invasion of Thyroid Carcinoma by Targeting miR-183-5p and miR-21 Frontiers In Endocrinology. 11: 136. https://doi.org/10.3389/fendo.2020.00136 |
| [56] | Zhou, Z., et al. (2021) Zebrafish otud6b Negatively Regulates Antiviral Responses by Suppressing K63-Linked Ubiquitination of irf3 and irf7 Journal of Immunology (Baltimore, Md.: 1950). 207(1): 244-256. https://doi.org/10.4049/jimmunol.2000891 |
| [57] | Averbeck, N., et al. (2008) Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation Molecular Biology of the Cell. 19(5): 2169-2178. https://doi.org/10.1091/mbc.E07-10-1077 |
| [58] | Enesa, K. and P. Evans (2014) The biology of A20-like molecules Advances In Experimental Medicine and Biology. 809: 33-48 |
| [59] | Duy, P. N., et al. (2019) Regulation of NF-κB- and STAT1-mediated plasmacytoid dendritic cell functions by A20 PloS One. 14(9): e0222697. https://doi.org/10.1371/journal.pone.0222697 |
| [60] | Mooney, E. C. and S. E. Sahingur (2021) The Ubiquitin System and A20: Implications in Health and Disease Journal of Dental Research. 100(1): 10-20. https://doi.org/10.1177/0022034520949486 |
| [61] | Martens, A. and G. van Loo (2020) A20 at the Crossroads of Cell Death, Inflammation, and Autoimmunity Cold Spring Harbor Perspectives In Biology. 12(1). https://doi.org/10.1101/cshperspect.a036418 |
| [62] | Hu, H., et al. (2013) OTUD7B controls non-canonical NF-κB activation through deubiquitination of TRAF3 Nature. 494(7437): 371-374. https://doi.org/10.1038/nature11831 |
| [63] | Zhang, J., et al. (2022) OTUD7B (Cezanne) ameliorates fibrosis after myocardial infarction via FAK-ERK/P38 MAPK signaling pathway Archives of Biochemistry and Biophysics. 724: 109266. https://doi.org/10.1016/j.abb.2022.109266 |
| [64] | Hu, H., et al. (2016) Otud7b facilitates T cell activation and inflammatory responses by regulating Zap70 ubiquitination The Journal of Experimental Medicine. 213(3): 399-414. https://doi.org/10.1084/jem.20151426 |
| [65] | Bremm, A., et al. (2014) Cezanne (OTUD7B) regulates HIF-1α homeostasis in a proteasome-independent manner EMBO Reports. 15(12): 1268-1277. https://doi.org/10.15252/embr.201438850 |
| [66] | Cui, C.-P., et al. (2018) Dynamic ubiquitylation of Sox2 regulates proteostasis and governs neural progenitor cell differentiation Nature Communications. 9(1): 4648. https://doi.org/10.1038/s41467-018-07025-z |
| [67] | Xu, Z., et al. (2014) Snail1-dependent transcriptional repression of Cezanne2 in hepatocellular carcinoma Oncogene. 33(22): 2836-2845. https://doi.org/10.1038/onc.2013.243 |
| [68] | Wu, X., et al. (2019) Crosstalk between Lys63- and Lys11-polyubiquitin signaling at DNA damage sites is driven by Cezanne Genes & Development. 33(23-24): 1702-1717. https://doi.org/10.1101/gad.332395.119 |
| [69] | Jin, J., et al. (2016) Epigenetic regulation of the expression of Il12 and Il23 and autoimmune inflammation by the deubiquitinase Trabid Nature Immunology. 17(3): 259-268. https://doi.org/10.1038/ni.3347 |
| [70] | Zhu, Y., et al. (2019) Trabid inhibits hepatocellular carcinoma growth and metastasis by cleaving RNF8-induced K63 ubiquitination of Twist1 Cell Death and Differentiation. 26(2): 306-320. https://doi.org/10.1038/s41418-018-0119-2 |
| [71] | Chen, Y.-H., et al. (2021) VPS34 K29/K48 branched ubiquitination governed by UBE3C and TRABID regulates autophagy, proteostasis and liver metabolism Nature Communications. 12(1): 1322. https://doi.org/10.1038/s41467-021-21715-1 |
| [72] | Zhang, X., H. Zhang, and Y. Wang (2014) Phosphorylation regulates VCIP135 function in Golgi membrane fusion during the cell cycle Journal of Cell Science. 127(Pt 1): 172-181. https://doi.org/10.1242/jcs.134668 |
| [73] | Totsukawa, G., et al. (2011) VCIP135 deubiquitinase and its binding protein, WAC, in p97ATPase-mediated membrane fusion The EMBO Journal. 30(17): 3581-3593. https://doi.org/10.1038/emboj.2011.260 |
| [74] | Verboom, L., E. Hoste, and G. van Loo (2021) OTULIN in NF-κB signaling, cell death, and disease Trends In Immunology. 42(7): 590-603. https://doi.org/10.1016/j.it.2021.05.003 |
| [75] | Chu, Y., et al. (2021) LUBAC and OTULIN regulate autophagy initiation and maturation by mediating the linear ubiquitination and the stabilization of ATG13 Autophagy. 17(7): 1684-1699. https://doi.org/10.1080/15548627.2020.1781393 |
| [76] | Heger, K., et al. (2018) OTULIN limits cell death and inflammation by deubiquitinating LUBAC Nature. 559(7712): 120-124. https://doi.org/10.1038/s41586-018-0256-2 |
| [77] | Schünke, H., et al. (2021) OTULIN inhibits RIPK1-mediated keratinocyte necroptosis to prevent skin inflammation in mice Nature Communications. 12(1): 5912. https://doi.org/10.1038/s41467-021-25945-1 |
| [78] | Luo, Z., et al. (2021) Exosomal OTULIN from M2 macrophages promotes the recovery of spinal cord injuries via stimulating Wnt/β-catenin pathway-mediated vascular regeneration Acta Biomaterialia. 136: 519-532. https://doi.org/10.1016/j.actbio.2021.09.026 |
| [79] | Piao, S., et al. (2017) Ovarian tumor domain-containing protein 1 deubiquitinates and stabilizes p53 Cellular Signalling. 33: 22-29. https://doi.org/10.1016/j.cellsig.2017.02.011 |
| [80] | Pu, Q., et al. (2020) Tumor suppressor OTUD3 induces growth inhibition and apoptosis by directly deubiquitinating and stabilizing p53 in invasive breast carcinoma cells BMC Cancer. 20(1): 583. https://doi.org/10.1186/s12885-020-07069-9 |
| [81] | Wu, Z., et al. (2019) OTU deubiquitinase 4 is silenced and radiosensitizes non-small cell lung cancer cells via inhibiting DNA repair Cancer Cell Int. 19: 99. https://doi.org/10.1186/s12935-019-0816-z |
| [82] | Luo, J., et al. (2013) OTUD5 regulates p53 stability by deubiquitinating p53 PloS One. 8(10): e77682. https://doi.org/10.1371/journal.pone.0077682 |
| [83] | Harhaj, E. W. and V. M. Dixit (2011) Deubiquitinases in the regulation of NF-κB signaling Cell Research. 21(1): 22-39. https://doi.org/10.1038/cr.2010.166 |
| [84] | González-Navajas, J. M., et al. (2010) Interleukin 1 receptor signaling regulates DUBA expression and facilitates Toll-like receptor 9-driven antiinflammatory cytokine production The Journal of Experimental Medicine. 207(13): 2799-2807. https://doi.org/10.1084/jem.20101326 |
| [85] | McNally, R. S., et al. (2011) DJ-1 enhances cell survival through the binding of Cezanne, a negative regulator of NF-kappaB The Journal of Biological Chemistry. 286(6): 4098-4106. https://doi.org/10.1074/jbc.M110.147371 |
| [86] | Harhaj, E. W. and V. M. Dixit (2012) Regulation of NF-κB by deubiquitinases Immunological Reviews. 246(1): 107-124. https://doi.org/10.1111/j.1600-065X.2012.01100.x |
| [87] | Wertz, I. E., et al. (2004) De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling Nature. 430(7000): 694-699 |
| [88] | Takiuchi, T., et al. (2014) Suppression of LUBAC-mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN Genes To Cells: Devoted To Molecular & Cellular Mechanisms. 19(3): 254-272. https://doi.org/10.1111/gtc.12128 |
| [89] | Nakamura, B. N., et al. (2018) A20 regulates canonical wnt-signaling through an interaction with RIPK4 PLoS One. 13(5): e0195893. https://doi.org/10.1371/journal.pone.0195893 |
| [90] | Wang, W. and Z. H. Wu (2020) OTULIN couples WNT signaling to resistance in triple-negative breast cancer Mol Cell Oncol. 7(6): 1825904. https://doi.org/10.1080/23723556.2020.1825904 |
| [91] | Yin, F., et al. (2019) Effect of Deubiquitinase Ovarian Tumor Domain-Containing Protein 5 (OTUD5) on Radiosensitivity of Cervical Cancer by Regulating the Ubiquitination of Akt and its Mechanism Medical Science Monitor: International Medical Journal of Experimental and Clinical Research. 25: 3469-3475. https://doi.org/10.12659/MSM.912904 |
| [92] | Shi, Y., et al. (2021) The dual roles of A20 in cancer Cancer Letters. 511: 26-35. https://doi.org/10.1016/j.canlet.2021.04.017 |
| [93] | Liu, W., et al. (2022) OTUD1 stabilizes PTEN to inhibit the PI3K/AKT and TNF-alpha/NF-kappaB signaling pathways and sensitize ccRCC to TKIs International Journal of Biological Sciences. 18(4): 1401-1414. https://doi.org/10.7150/ijbs.68980 |
| [94] | Lee, J., et al. (2018) Genome-wide association analysis identifies multiple loci associated with kidney disease-related traits in Korean populations PloS One. 13(3): e0194044. https://doi.org/10.1371/journal.pone.0194044 |
| [95] | Huijun, W., et al. (2005) Ex vivo transfer of the decorin gene into rat glomerulus via a mesangial cell vector suppressed extracellular matrix accumulation in experimental glomerulonephritis Experimental and Molecular Pathology. 78(1): 17-24 |
| [96] | Zhang, Y., et al. (2012) OTUB1 overexpression in mesangial cells is a novel regulator in the pathogenesis of glomerulonephritis through the decrease of DCN level PloS One. 7(1): e29654. https://doi.org/10.1371/journal.pone.0029654 |
| [97] | 梁雅灵, et al. (2016) 去泛素化酶A20在糖尿病肾病大鼠肾脏及脂多糖诱导的系膜细胞中的表达及变化 天津医药. 44(4): 444-448. https://doi.org/10.11958/20150120 |
| [98] | Linkermann, A., et al. (2014) Regulated cell death in AKI J Am Soc Nephrol. 25(12): 2689-701. https://doi.org/10.1681/ASN.2014030262 |
| [99] | 王涛, et al. (2022) 去泛素化酶OTUD6B截短体小鼠模型构建及表型初步分析 军事医学. 46(5): 355-360, 384. https://doi.org/10.7644/j.issn.1674⁃9960.2022.05.007 |
| [100] | Xu, L., et al. (2017) Silencing of OTUB1 inhibits migration of human glioma cells in vitro Neuropathology: Official Journal of the Japanese Society of Neuropathology. 37(3): 217-226. https://doi.org/10.1111/neup.12366 |
| [101] | Wang, P., et al. (2017) Tau interactome mapping based identification of Otub1 as Tau deubiquitinase involved in accumulation of pathological Tau forms in vitro and in vivo Acta Neuropathologica. 133(5): 731-749. https://doi.org/10.1007/s00401-016-1663-9 |
| [102] | 贾凤菊, 铁调节蛋白IRP2的去泛素化酶OTUD3鉴定及其在帕金森病黑质铁聚积中的作用研究. 2018, 青岛大学 |
| [103] | Voet, S., et al. (2018) A20 critically controls microglia activation and inhibits inflammasome-dependent neuroinflammation Nature Communications. 9(1): 2036. https://doi.org/10.1038/s41467-018-04376-5 |
| [104] | Mohebiany, A. N., et al. (2020) Microglial A20 Protects the Brain from CD8 T-Cell-Mediated Immunopathology Cell Reports. 30(5). https://doi.org/10.1016/j.celrep.2019.12.097 |
| [105] | Bao, Z., et al. (2019) Silencing of A20 Aggravates Neuronal Death and Inflammation After Traumatic Brain Injury: A Potential Trigger of Necroptosis Frontiers In Molecular Neuroscience. 12: 222. https://doi.org/10.3389/fnmol.2019.00222 |
| [106] | Longo, C. R., et al. (2003) A20 protects from CD40-CD40 ligand-mediated endothelial cell activation and apoptosis Circulation. 108(9): 1113-1118 |
| [107] | Qin, M., et al. (2017) Ginsenoside F1 Ameliorates Endothelial Cell Inflammatory Injury and Prevents Atherosclerosis in Mice through A20-Mediated Suppression of NF-kB Signaling Frontiers In Pharmacology. 8: 953. https://doi.org/10.3389/fphar.2017.00953 |
| [108] | Li, Y., et al. (2019) Preventing abnormal NF-κB activation and autoimmunity by Otub1-mediated p100 stabilization Cell Research. 29(6): 474-485. https://doi.org/10.1038/s41422-019-0174-3 |
| [109] | Graham, R. R., et al. (2008) Genetic variants near TNFAIP3 on 6q23 are associated with systemic lupus erythematosus Nature Genetics. 40(9): 1059-1061. https://doi.org/10.1038/ng.200 |
| [110] | Thomson, W., et al. (2007) Rheumatoid arthritis association at 6q23 Nature Genetics. 39(12): 1431-1433 |
| [111] | De Jager, P. L., et al. (2009) Meta-analysis of genome scans and replication identify CD6, IRF8 and TNFRSF1A as new multiple sclerosis susceptibility loci Nature Genetics. 41(7): 776-782. https://doi.org/10.1038/ng.401 |
| [112] | Vande Walle, L., et al. (2014) Negative regulation of the NLRP3 inflammasome by A20 protects against arthritis Nature. 512(7512): 69-73. https://doi.org/10.1038/nature13322 |
| [113] | Schlüter, D., et al. (2022) Ovarian tumor domain proteases in pathogen infection Trends In Microbiology. 30(1): 22-33. https://doi.org/10.1016/j.tim.2021.04.002 |
| [114] | Wang, S., et al. (2021) DDIT3 Targets Innate Immunity via the DDIT3-OTUD1-MAVS Pathway To Promote Bovine Viral Diarrhea Virus Replication J Virol. 95(6). https://doi.org/10.1128/JVI.02351-20 |
| [115] | Su, Y., et al. (2018) The Superimposed Deubiquitination Effect of OTULIN and Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) Nsp11 Promotes Multiplication of PRRSV Journal of Virology. 92(9). https://doi.org/10.1128/JVI.00175-18 |
| [116] | Lim, M. C. C., et al. (2017) Pathogen-induced ubiquitin-editing enzyme A20 bifunctionally shuts off NF-κB and caspase-8-dependent apoptotic cell death Cell Death and Differentiation. 24(9): 1621-1631. https://doi.org/10.1038/cdd.2017.89 |
| [117] | Uddin, M., et al. (2018) OTUD7A Regulates Neurodevelopmental Phenotypes in the 15q13.3 Microdeletion Syndrome American Journal of Human Genetics. 102(2): 278-295. https://doi.org/10.1016/j.ajhg.2018.01.006 |
| [118] | van Wijk, S. J. L., et al. (2017) Linear ubiquitination of cytosolic Salmonella Typhimurium activates NF-κB and restricts bacterial proliferation Nature Microbiology. 2: 17066. https://doi.org/10.1038/nmicrobiol.2017.66 |
| [119] | Liang, J., et al. (2020) The Ubiquitin-Modifying Enzyme A20 Terminates C-Type Lectin Receptor Signals and Is a Suppressor of Host Defense against Systemic Fungal Infection Infection and Immunity. 88(9). https://doi.org/10.1128/IAI.00048-20 |
| [120] | Nag, D. K. and D. Finley (2012) A small-molecule inhibitor of deubiquitinating enzyme USP14 inhibits Dengue virus replication Virus Research. 165(1): 103-106. https://doi.org/10.1016/j.virusres.2012.01.009 |
| [121] | Setz, C., et al. (2017) Inhibitors of Deubiquitinating Enzymes Block HIV-1 Replication and Augment the Presentation of Gag-Derived MHC-I Epitopes Viruses. 9(8). https://doi.org/10.3390/v9080222 |
| [122] | Cai, J., et al. (2019) PLGA nanoparticle-based docetaxel/LY294002 drug delivery system enhances antitumor activities against gastric cancer Journal of Biomaterials Applications. 33(10): 1394-1406. https://doi.org/10.1177/0885328219837683 |
