组蛋白去泛素化修饰的研究进展及其与肿瘤的关系_West China Medical Journal

Authors：

 王紫静 , 秦金玉 , 郭天娇 , 王一平 ,  杨锦林

四川大学华西医院消化内科, 成都 610041;

Corresponding author：

杨锦林, Email: mouse-577@163.com

Keywords：

表观遗传学; 组蛋白; 去泛素化; 肿瘤

DOI：

10.7507/1002-0179.20150565

Video：

Export PDF Favorites Scan Get Citation

Abstract Full text Figures/Tables Video References Cited by

组蛋白泛素化及去泛素化为两个可逆的过程，在基因转录后修饰以及细胞稳态的调控中起关键作用。组蛋白去泛素化可通过变化组蛋白修饰从而调控各种原癌基因及抑癌基因表达，使其在肿瘤的发生、发展中起重要作用，逐渐成为肿瘤治疗的研究热点。现就组蛋白去泛素化修饰相关内容及其在肿瘤发生发展中扮演的角色加以综述，为肿瘤的早期诊断和基因治疗提供新的途径和思路。

Citation： 王紫静, 秦金玉, 郭天娇, 王一平, 杨锦林. 组蛋白去泛素化修饰的研究进展及其与肿瘤的关系. West China Medical Journal, 2015, 30(10): 1979-1982. doi: 10.7507/1002-0179.20150565 Copy

1.	Kouzarides T. Chromatin modifications and their function[J]. Cell, 2007, 128(4):693-705.
2.	Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes[J]. Biochim Biophys Acta, 2004, 1695 (1/2/3):189-207.
3.	Suganuma T, Workman JL. Signals and combinatorial functions of histone modifications[J]. Annu Rev Bioche, 2011, 80:473-499.
4.	Hake SB, Xiao A, Allis CD. Linking the epigenetic "language" of covalent histone modifications to cancer[J]. Br J Cancer, 2004, 90(4):761-769.
5.	Misri S, Pandita S, Kumar R, et al. Telomeres, histone code, and DNA damage response[J]. Cytogenet Genome Res, 2008, 122(3/4):297-307.
6.	Strahl BD, Allis CD. The language of covalent histone modification[J]. Nature, 2000, 403(6765):41-45.
7.	Vijay-Kumar S, Bugg CE, Cook WJ. Structure of ubiquitin refined at 1.8 A resolution[J]. J Mol Biol, 1987, 194(3):531-544.
8.	Wilkinson KD. Ubiquitination and deubiquitination:targeting of proteins for degradation by the proteasome[J]. Semin Cell Dev Biol, 2000, 11(3):141-148.
9.	Oddo S. The ubiquitin-proteasome system in Alzheimer's disease[J]. J Cell Mol Med, 2008, 12(2):363-373.
10.	Chung CH, Baek SH. Deubiquitinating enzymes:their diversity and emerging roles[J]. Biochem Biophys Res Commun, 1999, 266(3):633-640.
11.	Lee D, Ezhkova E, Li B, et al. The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators[J]. Cell, 2005, 123(3):423-436.
12.	Swaminathan S, Amerik AY, Hochstrasser M. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast[J]. Mol Biol Cell, 1999, 10(8):2583-2594.
13.	Mueller RD,Yasuda H,Hatch CL, et al. Identification of ubiquitinated histones 2A and 2B in Physarum polycephalum. Disappearance of these proteins at metaphase and reappearance at anaphase[J]. J Biol Chem, 1985, 260 (8):5147-5153.
14.	Joo HY, Zhai L, Yang C, et al. Regulation of cell cycle progression and gene expression by H2A deubiquitination[J]. Nature, 2007, 449(7165):1068-1072.
15.	Ingvarsdottir K, Krogan NJ, Emre NC, et al. H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex[J]. Mol Cell Biol, 2005, 25(3):1162-1172.
16.	Emre NC, Ingvarsdottir K, Wyce A, et al. Maintenance of low histone ubiquitylation by Ubp10 correlates with telomere-proximal Sir2 association and gene silencing[J]. Mol Cell, 2005, 17(4):585-594.
17.	Weake VM, Lee KK, Guelman S, et al. SAGA-mediated H2B deubiquitination controls the development of neuronal connectivity in the Drosophila visual system[J]. EMBO J, 2008, 27(2):394-405.
18.	Lee HJ, Kim MS, Shin JM, et al. The expression patterns of deubiquitinating enzymes, USP22 and Usp22[J]. Gene Expr Patterns, 2006, 6(3):277-284.
19.	Atanassov BS, Evrard YA, Multani AS, et al. Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance[J]. Mol Cell, 2009, 35(3):352-364.
20.	Chipumuro E, Henriksen MA. The ubiquitin hydrolase USP22 contributes to 3'-end processing of JAK-STAT-inducible genes[J]. FASEB, 2012, 26(2):842-854.
21.	Marine JC, Francoz S, Maetens M, et al. Keeping p53 in check:essential and synergistic functions of Mdm² and Mdm4[J]. Cell Death Differ, 2006, 13(6):927-934.
22.	Li M, Chen D, Shiloh A, et al. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization[J]. Nature, 2002, 416(6881):648-653.
23.	Brooks CL, Li M, Hu M, et al. The p53——Mdm²——HAUSP complex is involved in p53 stabilization by HAUSP[J]. Oncogene, 2007, 26(51):7262-7266.
24.	Yuan J, Luo K, Zhang L, et al. USP10 regulates p53 localization and stability by deubiquitinating p53[J]. Cell, 2010, 140(3):384-396.
25.	Wicks SJ, Haros K, Maillard M, et al. The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling[J]. Oncogene, 2005, 24(54):8080-8084.
26.	叶盛威, 魏少忠. 泛素特异性蛋白酶2与肿瘤[J]. 肿瘤防治研究,2014, 41(5):505-508.
27.	Li J, Wang Z, Li Y. USP22 nuclear expression is significantly associated with progression and unfavorable clinical outcome inhuman esophageal squamous cell carcinoma[J]. J Cancer Res Clin Oncol, 2012, 138(8):1291-1297.
28.	Yang DD, Cui BB, Sun LY, et al. The co-expression of USP22 and BMI-1 may promote cancer progression and predict therapy failure in gastric carcinoma[J]. Cell Biochem Biophys, 2011, 61(3):703-710.
29.	Zhang Y, Yao L, Zhang X, et al. Elevated expression of USP22 in correlation with poor prognosis in patients with invasive breast cancer[J]. J Cancer Res Clin Oncol, 2011, 137(8):1245-1253.
30.	Xu H, Liu YL, Yang YM, et al. Knock-down of ubiquitin-specific protease 22 by micro-RNA interference inhibits coloretal cancer growth[J]. Int J Colorectal Dis, 2011, 27(1):21-30.
31.	Ricky WJ. Histone-deacetylase inhibitors:novel drugs for the treatment of cancer[J]. Nat Rev Drug Discov, 2002, 1(4):287-299.
32.	Johnsen SA. The enigmatic role of H2Bub1 in cancer[J]. FEBS Lett, 2012, 586(11):1592-601.
33.	罗朝蕊, 刘霆. 骨髓增生异常综合征去甲基化药物临床反应的生物学标志研究进展[J]. 华西医学, 2012, 27(5):779-782.

1. Kouzarides T. Chromatin modifications and their function[J]. Cell, 2007, 128(4):693-705.
2. Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes[J]. Biochim Biophys Acta, 2004, 1695 (1/2/3):189-207.
3. Suganuma T, Workman JL. Signals and combinatorial functions of histone modifications[J]. Annu Rev Bioche, 2011, 80:473-499.
4. Hake SB, Xiao A, Allis CD. Linking the epigenetic "language" of covalent histone modifications to cancer[J]. Br J Cancer, 2004, 90(4):761-769.
5. Misri S, Pandita S, Kumar R, et al. Telomeres, histone code, and DNA damage response[J]. Cytogenet Genome Res, 2008, 122(3/4):297-307.
6. Strahl BD, Allis CD. The language of covalent histone modification[J]. Nature, 2000, 403(6765):41-45.
7. Vijay-Kumar S, Bugg CE, Cook WJ. Structure of ubiquitin refined at 1.8 A resolution[J]. J Mol Biol, 1987, 194(3):531-544.
8. Wilkinson KD. Ubiquitination and deubiquitination:targeting of proteins for degradation by the proteasome[J]. Semin Cell Dev Biol, 2000, 11(3):141-148.
9. Oddo S. The ubiquitin-proteasome system in Alzheimer's disease[J]. J Cell Mol Med, 2008, 12(2):363-373.
10. Chung CH, Baek SH. Deubiquitinating enzymes:their diversity and emerging roles[J]. Biochem Biophys Res Commun, 1999, 266(3):633-640.
11. Lee D, Ezhkova E, Li B, et al. The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators[J]. Cell, 2005, 123(3):423-436.
12. Swaminathan S, Amerik AY, Hochstrasser M. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast[J]. Mol Biol Cell, 1999, 10(8):2583-2594.
13. Mueller RD,Yasuda H,Hatch CL, et al. Identification of ubiquitinated histones 2A and 2B in Physarum polycephalum. Disappearance of these proteins at metaphase and reappearance at anaphase[J]. J Biol Chem, 1985, 260 (8):5147-5153.
14. Joo HY, Zhai L, Yang C, et al. Regulation of cell cycle progression and gene expression by H2A deubiquitination[J]. Nature, 2007, 449(7165):1068-1072.
15. Ingvarsdottir K, Krogan NJ, Emre NC, et al. H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex[J]. Mol Cell Biol, 2005, 25(3):1162-1172.
16. Emre NC, Ingvarsdottir K, Wyce A, et al. Maintenance of low histone ubiquitylation by Ubp10 correlates with telomere-proximal Sir2 association and gene silencing[J]. Mol Cell, 2005, 17(4):585-594.
17. Weake VM, Lee KK, Guelman S, et al. SAGA-mediated H2B deubiquitination controls the development of neuronal connectivity in the Drosophila visual system[J]. EMBO J, 2008, 27(2):394-405.
18. Lee HJ, Kim MS, Shin JM, et al. The expression patterns of deubiquitinating enzymes, USP22 and Usp22[J]. Gene Expr Patterns, 2006, 6(3):277-284.
19. Atanassov BS, Evrard YA, Multani AS, et al. Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance[J]. Mol Cell, 2009, 35(3):352-364.
20. Chipumuro E, Henriksen MA. The ubiquitin hydrolase USP22 contributes to 3'-end processing of JAK-STAT-inducible genes[J]. FASEB, 2012, 26(2):842-854.
21. Marine JC, Francoz S, Maetens M, et al. Keeping p53 in check:essential and synergistic functions of Mdm² and Mdm4[J]. Cell Death Differ, 2006, 13(6):927-934.
22. Li M, Chen D, Shiloh A, et al. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization[J]. Nature, 2002, 416(6881):648-653.
23. Brooks CL, Li M, Hu M, et al. The p53——Mdm²——HAUSP complex is involved in p53 stabilization by HAUSP[J]. Oncogene, 2007, 26(51):7262-7266.
24. Yuan J, Luo K, Zhang L, et al. USP10 regulates p53 localization and stability by deubiquitinating p53[J]. Cell, 2010, 140(3):384-396.
25. Wicks SJ, Haros K, Maillard M, et al. The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-beta signalling[J]. Oncogene, 2005, 24(54):8080-8084.
26. 叶盛威, 魏少忠. 泛素特异性蛋白酶2与肿瘤[J]. 肿瘤防治研究,2014, 41(5):505-508.
27. Li J, Wang Z, Li Y. USP22 nuclear expression is significantly associated with progression and unfavorable clinical outcome inhuman esophageal squamous cell carcinoma[J]. J Cancer Res Clin Oncol, 2012, 138(8):1291-1297.
28. Yang DD, Cui BB, Sun LY, et al. The co-expression of USP22 and BMI-1 may promote cancer progression and predict therapy failure in gastric carcinoma[J]. Cell Biochem Biophys, 2011, 61(3):703-710.
29. Zhang Y, Yao L, Zhang X, et al. Elevated expression of USP22 in correlation with poor prognosis in patients with invasive breast cancer[J]. J Cancer Res Clin Oncol, 2011, 137(8):1245-1253.
30. Xu H, Liu YL, Yang YM, et al. Knock-down of ubiquitin-specific protease 22 by micro-RNA interference inhibits coloretal cancer growth[J]. Int J Colorectal Dis, 2011, 27(1):21-30.
31. Ricky WJ. Histone-deacetylase inhibitors:novel drugs for the treatment of cancer[J]. Nat Rev Drug Discov, 2002, 1(4):287-299.
32. Johnsen SA. The enigmatic role of H2Bub1 in cancer[J]. FEBS Lett, 2012, 586(11):1592-601.
33. 罗朝蕊, 刘霆. 骨髓增生异常综合征去甲基化药物临床反应的生物学标志研究进展[J]. 华西医学, 2012, 27(5):779-782.

Previous Article
抗磷脂综合征肾损害
Next Article
食管瘘治疗新进展

West China Medical Journal

组蛋白去泛素化修饰的研究进展及其与肿瘤的关系

Abstract Full text Figures/Tables Video References Cited by

Previous Article

Next Article

Format

Content