Advances in Deubiquitinating Enzyme Inhibition and Applications in Cancer Therapeutics

被引:108
作者
Antao, Ainsley Mike [1 ]
Tyagi, Apoorvi [1 ]
Kim, Kye-Seong [1 ,2 ]
Ramakrishna, Suresh [1 ,2 ]
机构
[1] Hanyang Univ, Grad Sch Biomed Sci & Engn, Seoul 04763, South Korea
[2] Hanyang Univ, Coll Med, Seoul 04763, South Korea
基金
新加坡国家研究基金会;
关键词
cancer therapy; deubiquitinase; DUB inhibitors; USPs phylogenetic tree; signaling pathways; NF-KAPPA-B; SMALL-MOLECULE INHIBITOR; UBIQUITIN-ACTIVATING ENZYME; FINGER PROTEIN A20; CELL-CYCLE ARREST; ACTIVE PROTEASOME INHIBITOR; GENOME-WIDE ASSOCIATION; I CLINICAL-TRIAL; TUMOR-SUPPRESSOR; MULTIPLE-MYELOMA;
D O I
10.3390/cancers12061579
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Since the discovery of the ubiquitin proteasome system (UPS), the roles of ubiquitinating and deubiquitinating enzymes (DUBs) have been widely elucidated. The ubiquitination of proteins regulates many aspects of cellular functions such as protein degradation and localization, and also modifies protein-protein interactions. DUBs cleave the attached ubiquitin moieties from substrates and thereby reverse the process of ubiquitination. The dysregulation of these two paramount pathways has been implicated in numerous diseases, including cancer. Attempts are being made to identify inhibitors of ubiquitin E3 ligases and DUBs that potentially have clinical implications in cancer, making them an important target in the pharmaceutical industry. Therefore, studies in medicine are currently focused on the pharmacological disruption of DUB activity as a rationale to specifically target cancer-causing protein aberrations. Here, we briefly discuss the pathophysiological and physiological roles of DUBs in key cancer-related pathways. We also discuss the clinical applications of promising DUB inhibitors that may contribute to the development of DUBs as key therapeutic targets in the future.
引用
收藏
页码:1 / 36
页数:34
相关论文
共 324 条
  • [61] Structure-based design of spiro-oxindoles as potent, specific small-molecule inhibitors of the MDM2-p53 interaction
    Ding, Ke
    Lu, Yipin
    Nikolovska-Coleska, Zaneta
    Wang, Guoping
    Qiu, Su
    Shangary, Sanjeev
    Gao, Wei
    Qin, Dongguang
    Stuckey, Jeanne
    Krajewski, Krzysztof
    Roller, Peter P.
    Wang, Shaomeng
    [J]. JOURNAL OF MEDICINAL CHEMISTRY, 2006, 49 (12) : 3432 - 3435
  • [62] Emerging principles in protease-based drug discovery
    Drag, Marcin
    Salvesen, Guy S.
    [J]. NATURE REVIEWS DRUG DISCOVERY, 2010, 9 (09) : 690 - 701
  • [63] USP10 deubiquitylates the histone variant H2A.Z and both are required for androgen receptor-mediated gene activation
    Draker, Ryan
    Sarcinella, Elizabeth
    Cheung, Peter
    [J]. NUCLEIC ACIDS RESEARCH, 2011, 39 (09) : 3529 - 3542
  • [64] Usp18 Regulates Epidermal Growth Factor (EGF) Receptor Expression and Cancer Cell Survival via MicroRNA-7
    Duex, Jason E.
    Comeau, Laurey
    Sorkin, Alexander
    Purow, Benjamin
    Kefas, Benjamin
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2011, 286 (28) : 25377 - 25386
  • [65] RNA Interference Screen Identifies Usp18 as a Regulator of Epidermal Growth Factor Receptor Synthesis
    Duex, Jason E.
    Sorkin, Alexander
    [J]. MOLECULAR BIOLOGY OF THE CELL, 2009, 20 (06) : 1833 - 1844
  • [66] FAM/USP9x, a Deubiquitinating Enzyme Essential for TGFβ Signaling, Controls Smad4 Monoubiquitination
    Dupont, Sirio
    Mamidi, Anant
    Cordenonsi, Michelangelo
    Montagner, Marco
    Zacchigna, Luca
    Adorno, Maddalena
    Martello, Graziano
    Stinchfield, Michael J.
    Soligo, Sandra
    Morsut, Leonardo
    Inui, Masafumi
    Moro, Stefano
    Modena, Nicola
    Argenton, Francesco
    Newfeld, Stuart J.
    Piccolo, Stefano
    [J]. CELL, 2009, 136 (01) : 123 - 135
  • [67] Differential expression and function of A20 and TRAF1 in Hodgkin lymphoma and anaplastic large cell lymphoma and their induction by CD30 stimulation
    Dürkop, H
    Hirsch, B
    Hahn, C
    Foss, HD
    Stein, H
    [J]. JOURNAL OF PATHOLOGY, 2003, 200 (02) : 229 - 239
  • [68] USP15 stabilizes TGF-β receptor I and promotes oncogenesis through the activation of TGF-β signaling in glioblastoma
    Eichhorn, Pieter J. A.
    Rodon, Laura
    Gonzalez-Junca, Alba
    Dirac, Annette
    Gili, Maguei
    Martinez-Saez, Elena
    Aura, Claudia
    Barba, Ignasi
    Peg, Vicente
    Prat, Aleix
    Cuartas, Isabel
    Jimenez, Jose
    Garcia-Dorado, David
    Sahuquillo, Juan
    Bernards, Rene
    Baselga, Jose
    Seoane, Joan
    [J]. NATURE MEDICINE, 2012, 18 (03) : 429 - U192
  • [69] NF-κB suppression by the deubiquitinating enzyme Cezanne -: A novel negative feedback loop in pro-inflammatory signaling
    Enesa, Karine
    Zakkar, Mustafa
    Chaudhury, Hera
    Luong, Le A.
    Rawlinson, Lesley
    Mason, Justin C.
    Haskard, Dorian O.
    Dean, Jonathan L. E.
    Evans, Paul C.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (11) : 7036 - 7045
  • [70] Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity
    Evans, PC
    Ovaa, H
    Hamon, M
    Kilshaw, PJ
    Hamm, S
    Bauer, S
    Ploegh, HL
    Smith, TS
    [J]. BIOCHEMICAL JOURNAL, 2004, 378 : 727 - 734