去泛素化酶家族在头颈部肿瘤中的研究进展
摘要
目标蛋白质在细胞内的定位、稳定性和功能。去泛素化过程涉及组蛋白修饰、细胞周期调节、细胞分化、细胞凋亡、内吞、
自噬以及 DNA 损伤后的修复。此外，它还参与了癌变和癌症发展过程。在本综述中，我们将讨论这些问题，以了解去泛
素化酶（DUB）在头颈部肿瘤中的功能。为进一步发现患者的潜在治疗策略。
关键词
全文:
PDF参考
[1]POZHIDAEVA A, BEZSONOVA I. USP7: Structure, substrate
specificity, and inhibition [J]. DNA Repair (Amst), 2019, 76: 30-9.
[2]KOMANDER D, RAPE M. The ubiquitin code [J]. Annu
Rev Biochem, 2012, 81: 203-29.
[3]PENG J, SCHWARTZ D, ELIAS J E, et al. A proteomics
approach to understanding protein ubiquitination [J]. Nat
Biotechnol, 2003, 21(8): 921-6.
[4]XU D, YUAN L, LIU X, et al. EphB6 overexpression and
Apc mutation together promote colorectal cancer [J]. Oncotarget,
2016, 7(21): 31111-21.
[5]MUKHOPADHYAY D, RIEZMAN H. Proteasomeindependent functions of ubiquitin in endocytosis and signaling [J].
Science, 2007, 315(5809): 201-5.
[6]WANG G, GAO Y, LI L, et al. K63-linked ubiquitination
in kinase activation and cancer [J]. Front Oncol, 2012, 2: 5.
[7]WU C J, CONZE D B, LI T, et al. Sensing of Lys 63-linked
polyubiquitination by NEMO is a key event in NF-kappaB activation
[corrected] [J]. Nat Cell Biol, 2006, 8(4): 398-406.
[8]SRIVASTAVA D, CHAKRABARTI O. Mahoguninmediated α-tubulin ubiquitination via noncanonical K6 linkage
regulates microtubule stability and mitotic spindle orientation [J].
Cell Death Dis, 2014, 5(2): e1064.
[9]LIU J, HAN C, XIE B, et al. Rhbdd3 controls
autoimmunity by suppressing the production of IL-6 by dendritic
cells via K27-linked ubiquitination of the regulator NEMO [J]. Nat
Immunol, 2014, 15(7): 612-22.
[10]ELIA A E, BOARDMAN A P, WANG D C, et al.
Quantitative Proteomic Atlas of Ubiquitination and Acetylation in
the DNA Damage Response [J]. Mol Cell, 2015, 59(5): 867-81.
[11]LIN M, ZHAO Z, YANG Z, et al. USP38 Inhibits Type
I Interferon Signaling by Editing TBK1 Ubiquitination through
NLRP4 Signalosome [J]. Mol Cell, 2016, 64(2): 267-81.
[12]FARSHI P, DESHMUKH R R, NWANKWO J O, et al.
Deubiquitinases (DUBs) and DUB inhibitors: a patent review [J].
Expert Opin Ther Pat, 2015, 25(10): 1191-208.
[13]PFOH R, LACDAO I K, SARIDAKIS V. Deubiquitinases
and the new therapeutic opportunities offered to cancer [J]. Endocr
Relat Cancer, 2015, 22(1): T35-54.
[14]CLERICI M, LUNA-VARGAS M P, FAESEN A C, et al.
The DUSP-Ubl domain of USP4 enhances its catalytic efficiency
by promoting ubiquitin exchange [J]. Nat Commun, 2014, 5: 5399.
[15]BLANDINO G, DI AGOSTINO S. New therapeutic
strategies to treat human cancers expressing mutant p53 proteins
[J]. J Exp Clin Cancer Res, 2018, 37(1): 30.
[16]WU D, PRIVES C. Relevance of the p53-MDM2 axis to
aging [J]. Cell Death Differ, 2018, 25(1): 169-79.
[17]YUAN J, LUO K, ZHANG L, et al. USP10 regulates p53
localization and stability by deubiquitinating p53 [J]. Cell, 2010,
140(3): 384-96.
[18]ZOU Q, JIN J, HU H, et al. USP15 stabilizes MDM2
to mediate cancer-cell survival and inhibit antitumor T cell
responses [J]. Nat Immunol, 2014, 15(6): 562-70.
[19]SUN X X, CHALLAGUNDLA K B, DAI M S. Positive
regulation of p53 stability and activity by the deubiquitinating
enzyme Otubain 1 [J]. Embo j, 2012, 31(3): 576-92.
[20]CARNEIRO A P, REIS C F, MORARI E C, et al. A
putative OTU domain-containing protein 1 deubiquitinating
enzyme is differentially expressed in thyroid cancer and identifies
less-aggressive tumours [J]. Br J Cancer, 2014, 111(3): 551-8.
[21]TAVANA O, LI D, DAI C, et al. HAUSP deubiquitinates and
stabilizes N-Myc in neuroblastoma [J]. Nat Med, 2016, 22(10): 1180-6.
[22]WU H T, KUO Y C, HUNG J J, et al. K63-
polyubiquitinated HAUSP deubiquitinates HIF-1α and
dictates H3K56 acetylation promoting hypoxia-induced tumour
progression [J]. Nat Commun, 2016, 7: 13644.
[23]WANG Q, MA S, SONG N, et al. Stabilization of histone
demethylase PHF8 by USP7 promotes breast carcinogenesis [J]. J
Clin Invest, 2016, 126(6): 2205-20.
[24]LI J, DAI Y, GE H, et al. The deubiquitinase USP7
promotes HNSCC progression via deubiquitinating and stabilizing
TAZ [J]. Cell Death Dis, 2022, 13(8): 677.
[25]ZHANG X Y, PFEIFFER H K, THORNE A W, et al.
USP22, an hSAGA subunit and potential cancer stem cell marker,
reverses the polycomb-catalyzed ubiquitylation of histone H2A [J].
Cell Cycle, 2008, 7(11): 1522-4.
[26]ZHANG X Y, VARTHI M, SYKES S M, et al. The
putative cancer stem cell marker USP22 is a subunit of the human
SAGA complex required for activated transcription and cell-cycle
progression [J]. Mol Cell, 2008, 29(1): 102-11.
[27]LEE H J, KIM M S, SHIN J M, et al. The expression
patterns of deubiquitinating enzymes, USP22 and Usp22 [J]. Gene
Expr Patterns, 2006, 6(3): 277-84.
[28] 孙晓梅 , 段晓峰 . 去泛素化酶在口腔鳞癌中的研究
进展 [J]. 中国口腔颌面外科杂志 , 2024, 22(03): 294-9.
[29] 丁宁枫 . 结肠癌中去泛素化酶 USP22 调控癌基因
SRC 的分子机制研究 [D], 2023.
[30]LIU T, LIU J, CHEN Q, et al. Expression of USP22 and
the chromosomal passenger complex is an indicator of malignant
progression in oral squamous cell carcinoma [J]. Oncol Lett, 2019,
17(2): 2040-6.
[31]KOVALENKO A, CHABLE-BESSIA C, CANTARELLA
G, et al. The tumour suppressor CYLD negatively regulates
NF-kappaB signalling by deubiquitination [J]. Nature, 2003,
424(6950): 801-5.
[32]VERHOEFT K R, NGAN H L, LUI V W Y. The
cylindromatosis (CYLD) gene and head and neck tumorigenesis [J].
Cancers Head Neck, 2016, 1: 10.
[33]CUI Z, KANG H, GRANDIS J R, et al. CYLD Alterations
in the Tumorigenesis and Progression of Human PapillomavirusAssociated Head and Neck Cancers [J]. Mol Cancer Res, 2021,
19(1): 14-24.
[34]COURTOIS G. Tumor suppressor CYLD: negative
regulation of NF-kappaB signaling and more [J]. Cell Mol Life Sci,
2008, 65(7-8): 1123-32.
[35]JONES M H, FURLONG R A, BURKIN H, et al. The
Drosophila developmental gene fat facets has a human homologue
in Xp11.4 which escapes X-inactivation and has related
sequences on Yq11.2 [J]. Hum Mol Genet, 1996, 5(11): 1695-701.
[36]SCHWICKART M, HUANG X, LILL J R, et al.
Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell
survival [J]. Nature, 2010, 463(7277): 103-7.
[37]COX J L, WILDER P J, WUEBBEN E L, et al. Contextdependent function of the deubiquitinating enzyme USP9X in
pancreatic ductal adenocarcinoma [J]. Cancer Biol Ther, 2014,
15(8): 1042-52.
[38] 芦文萱 , 唐伏秋 , 杨波 . 去泛素化酶 USP9X 在结肠癌
组织中的表达及意义 [J]. 现代肿瘤医学 , 2020, 28(01): 88-91.
[39]HIJIOKA H, SETOGUCHI T, MIYAWAKI A, et al.
Upregulation of Notch pathway molecules in oral squamous cell
carcinoma [J]. Int J Oncol, 2010, 36(4): 817-22.
(15 摘要 Views, 21 PDF Downloads)
Refbacks
- 当前没有refback。