Power and promise of ubiquitin carboxyl-terminal hydrolase 37 as a target of cancer therapy

Asian Pacific Journal of Cancer Prevention

Volumn 14, Issue 4, 2013, Pages 2173-2179

  Chen, Yan Jie ^a   Ma, Yu Shui ^a   Fang, Ying ^a   Wang, Yi ^a   Fu, Da ^a   Shen, Xi Zhong ^a  

^a ZHONGSHAN HOSPITAL OF FUDAN UNIVERSITY   (China)

Author keywords

Deubiquitination; Proteasome; Protein interaction; Tumor therapy target; UCH37

Indexed keywords

ANTINEOPLASTIC AGENT; UBIQUITIN THIOLESTERASE; UCH37 PROTEIN, MOUSE; UCHL5 PROTEIN, HUMAN;

ANIMAL; DRUG ANTAGONISM; ENZYMOLOGY; HUMAN; MOLECULARLY TARGETED THERAPY; MOUSE; NEOPLASM; REVIEW;

ANIMALS; ANTINEOPLASTIC AGENTS; HUMANS; MICE; MOLECULAR TARGETED THERAPY; NEOPLASMS; UBIQUITIN THIOLESTERASE;

EID: 84880278583     PISSN: 15137368     EISSN: 2476762X     Source Type: Journal    
DOI: 10.7314/APJCP.2013.14.4.2173     Document Type: Review

References (62)

1. Al-Shami A, Jhaver KG, Vogel P, et al (2010). Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development. PLoS One, 5, e13654.
2. Baek D, Villen J, Shin C, et al (2008). The impact of microRNAs on protein output. Nature, 455, 64-71.
3. Betel D, Wilson M, Gabow A, Marks DS, Sander C (2008). The microRNA.org resource: targets and expression. Nucleic Acids Res, 36, D149-53.
4. Blom N, Gammeltoft S, Brunak S (1999). Sequence and structurebased prediction of eukaryotic protein phosphorylation sites. J Mol Biol, 294, 1351-62.
5. Burgie SE, Bingman CA, Soni AB, Phillips GN, Jr. (2011). Structural characterization of human Uch37. Proteins.
6. Cai Y, Jin J, Yao T, et al (2007). YY1 functions with INO80 to activate transcription. Nat Struct Mol Biol, 14, 872-4.
7. Chen X, Lee BH, Finley D, Walters KJ (2010). Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. Mol Cell, 38, 404-15.
8. Chen Y, Fu D, Xi J, et al (2012). Expression and Clinical Significance of UCH37 in Human Esophageal Squamous Cell Carcinoma. Dig Dis Sci, 57, 2310-7.
9. Chen Z, Niu X, Li Z, et al (2011). Effect of ubiquitin carboxyterminal hydrolase 37 on apoptotic in A549 cells. Cell Biochem Funct, 29, 142-8.
10. Chung CH, Baek SH (1999). Deubiquitinating enzymes: their diversity and emerging roles. Biochem Biophys Res Commun, 266, 633-40.
11. Cutts AJ, Soond SM, Powell S, Chantry A (2011). Early phase TGFbeta receptor signalling dynamics stabilised by the deubiquitinase UCH37 promotes cell migratory responses. Int J Biochem Cell Biol, 43, 604-12.
12. D'Arcy P, Brnjic S, Olofsson MH, et al (2011). Inhibition of proteasome deubiquitinating activity as a new cancer therapy. Nat Med, 17, 1636-40.
13. Deveraux Q, Ustrell V, Pickart C, Rechsteiner M (1994). A 26 S protease subunit that binds ubiquitin conjugates. J Biol Chem, 269, 7059-61.
14. Fang Y, Fu D, Shen XZ (2010). The potential role of ubiquitin c-terminal hydrolases in oncogenesis. Biochim Biophys Acta, 1806, 1-6.
15. Fang Y, Fu D, Tang W, et al (2013). Ubiquitin C-terminal Hydrolase 37, a novel predictor for hepatocellular carcinoma recurrence, promotes cell migration and invasion via interacting and deubiquitinating PRP19. Biochim Biophys Acta, 1833, 559-72.
16. Fang Y, Mu J, Ma Y, et al (2012). The interaction between ubiquitin C-terminal hydrolase 37 and glucose-regulated protein 78 in hepatocellular carcinoma. Mol Cell Biochem, 359, 59-66.
17. Friedman RC, Farh KK, Burge CB, Bartel DP (2009). Most mammalian mRNAs are conserved targets of microRNAs. Genome Res, 19, 92-105.
18. Glickman MH, Ciechanover A (2002). The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev, 82, 373-428.
19. Goldberg AL (2003). Protein degradation and protection against misfolded or damaged proteins. Nature, 426, 895-9.
20. Guterman A, Glickman MH (2004). Deubiquitinating enzymes are IN/(trinsic to proteasome function). Curr Protein Pept Sci, 5, 201-11.
21. Hamazaki J, Iemura S, Natsume T, et al (2006). A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J, 25, 4524-36.
22. Hanna J, Hathaway NA, Tone Y, et al (2006). Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell, 127, 99-111.
23. Hershko A and Ciechanover A (1998). The ubiquitin system. Annu Rev Biochem, 67, 425-79.
24. Hirohashi Y, Wang Q, Liu Q, et al (2006). p78/MCRS1 forms a complex with centrosomal protein Nde1 and is essential for cell viability. Oncogene, 25, 4937-46.
25. Holzl H, Kapelari B, Kellermann J, et al (2000). The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitylating enzyme. J Cell Biol, 150, 119-30.
26. Husnjak K, Elsasser S, Zhang N, et al (2008). Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature, 453, 481-8.
27. Jacobson AD, Zhang NY, Xu P, et al (2009). The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome. J Biol Chem, 284, 35485-94.
28. Kapuria V, Peterson LF, Fang D, et al (2010). Deubiquitinase inhibition by small-molecule WP1130 triggers aggresome formation and tumor cell apoptosis. Cancer Res, 70, 9265- 76.
29. Koulich E, Li X, DeMartino GN (2008). Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol Biol Cell, 19, 1072-82.
30. Lam YA, DeMartino GN, Pickart CM, Cohen RE (1997a). Specificity of the ubiquitin isopeptidase in the PA700 regulatory complex of 26 S proteasomes. J Biol Chem, 272, 28438-46.
31. Lam YA, Xu W, DeMartino GN, Cohen RE (1997b). Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature, 385, 737-40.
32. Larkin MA, Blackshields G, Brown NP, et al (2007). Clustal W and Clustal X version 2.0. Bioinformatics, 23, 2947-8.
33. Lee BH, Lee MJ, Park S, et al (2010). Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature, 467, 179-84.
34. Lee MJ, Lee BH, Hanna J, King RW, Finley D (2011). Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol Cell Proteomics, 10, R110003871.
35. Li T, Duan W, Yang H, et al (2001). Identification of two proteins, S14 and UIP1, that interact with UCH37. FEBS Lett, 488, 201-5.
36. Liu CH, Goldberg AL, Qiu XB (2007). New insights into the role of the ubiquitin-proteasome pathway in the regulation of apoptosis. Chang Gung Med J, 30, 469-79.
37. Mazumdar T, Gorgun FM, Sha Y, et al (2010). Regulation of NF-kappaB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13). Proc Natl Acad Sci U S A, 107, 13854-9.
38. Nishio K, Kim SW, Kawai K, et al (2009). Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain. Biochem Biophys Res Commun, 390, 855-60.
39. Peth A, Besche HC, Goldberg AL (2009). Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening. Mol Cell, 36, 794-804.
40. Peth A, Kukushkin N, Bosse M, Goldberg AL (2013). Ubiquitinated proteins activate the proteasomal ATPases by binding to Usp14 or Uch37. J Biol Chem, 288, 7781-90.
41. Pickart CM (2001). Mechanisms underlying ubiquitination. Annu Rev Biochem, 70, 503-33.
42. Qiu XB, Ouyang SY, Li CJ, et al (2006). hRpn13/ADRM1/ GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J, 25, 5742-53.
43. Reese MG (2001). Application of a time-delay neural network to promoter annotation in the Drosophila melanogaster genome. Comput Chem, 26, 51-6.
44. Rolen U, Kobzeva V, Gasparjan N, et al (2006). Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines. Mol Carcinog, 45, 260-9.
45. Saeki Y, Tanaka K (2008). Cell biology: two hands for degradation. Nature, 453, 460-1.
46. Schreiner P, Chen X, Husnjak K, et al (2008). Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature, 453, 548-52.
47. Stone M, Hartmann-Petersen R, Seeger M, et al (2004). Uch2/ Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast. J Mol Biol, 344, 697-706.
48. Sulewska A, Niklinska W, Kozlowski M, et al (2007). DNA methylation in states of cell physiology and pathology. Folia Histochem Cytobiol, 45, 149-58.
49. The PyMOL Molecular Graphics System: [http://www.pymol.org/citing], Version 1.3, http://www.pymol.org/export.
50. Verma R, Aravind L, Oania R, et al (2002). Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science, 298, 611-5.
51. Wang X (2008). miRDB: a microRNA target prediction and functional annotation database with a wiki interface. RNA, 14, 1012-7.
52. Wang X, El Naqa IM (2008). Prediction of both conserved and nonconserved microRNA targets in animals. Bioinformatics, 24, 325-32.
53. Wicks SJ, Grocott T, Haros K, et al (2006). Reversible ubiquitination regulates the Smad/TGF-beta signalling pathway. Biochem Soc Trans, 34, 761-3.
54. Wicks SJ, Haros K, Maillard M, et al (2005). The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGFbeta signalling. Oncogene, 24, 8080-4.
55. Wilkinson KD (1997). Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J, 11, 1245-56.
56. Wilkinson KD (2002). Cell biology: unchaining the condemned. Nature, 419, 351-3.
57. Wong YH, Lee TY, Liang HK, et al (2007). KinasePhos 2.0: a web server for identifying protein kinase-specific phosphorylation sites based on sequences and coupling patterns. Nucleic Acids Res, 35, W588-94.
58. Yao T, Cohen RE (2002). A cryptic protease couples deubiquitination and degradation by the proteasome. Nature, 419, 403-7.
59. Yao T, Song L, Jin J, et al (2008). Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex. Mol Cell, 31, 909-17.
60. Yao T, Song L, Xu W, et al (2006). Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nat Cell Biol, 8, 994-1002.
61. Zediak VP, Berger SL (2008). Hit and run: transient deubiquitylase activity in a chromatin-remodeling complex. Mol Cell, 31, 773-4.
62. Zhou ZR, Zhang YH, Liu S, Song AX, Hu HY (2011). Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains. Biochem J, 441, 143-9.