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翻译后修饰、SUMOylation 和癌症(综述)。

The post-translational modification, SUMOylation, and cancer (Review).

机构信息

Key Laboratory of the Digestive System Tumors of Gansu Province, Second Hospital of Lanzhou University, Lanzhou, Gansu 730030, P.R. China.

Department of General Surgery, Second Hospital of Lanzhou University, Lanzhou, Gansu 730030, P.R. China.

出版信息

Int J Oncol. 2018 Apr;52(4):1081-1094. doi: 10.3892/ijo.2018.4280. Epub 2018 Feb 22.

DOI:10.3892/ijo.2018.4280
PMID:29484374
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5843405/
Abstract

SUMOylation is a reversible post-translational modification which has emerged as a crucial molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune responses, carcinogenesis, cell cycle progression and apoptosis. Four SUMO isoforms have been identified, which are SUMO1, SUMO2/3 and SUMO4. The small ubiquitin-like modifier (SUMO) pathway is conserved in all eukaryotes and plays pivotal roles in the regulation of gene expression, cellular signaling and the maintenance of genomic integrity. The SUMO catalytic cycle includes maturation, activation, conjugation, ligation and de-modification. The dysregulation of the SUMO system is associated with a number of diseases, particularly cancer. SUMOylation is widely involved in carcinogenesis, DNA damage response, cancer cell proliferation, metastasis and apoptosis. SUMO can be used as a potential therapeutic target for cancer. In this review, we briefly outline the basic concepts of the SUMO system and summarize the involvement of SUMO proteins in cancer cells in order to better understand the role of SUMO in human disease.

摘要

SUMOylation 是一种可逆的翻译后修饰,已成为一种关键的分子调节机制,参与 DNA 损伤修复、免疫反应、肿瘤发生、细胞周期进程和细胞凋亡的调节。已经鉴定出四种 SUMO 同种型,即 SUMO1、SUMO2/3 和 SUMO4。小泛素样修饰物(SUMO)途径在所有真核生物中都保守,在基因表达、细胞信号转导和基因组完整性的维持中发挥关键作用。SUMO 的催化循环包括成熟、激活、缀合、连接和去修饰。SUMO 系统的失调与许多疾病,特别是癌症有关。SUMOylation 广泛参与肿瘤发生、DNA 损伤反应、癌细胞增殖、转移和凋亡。SUMO 可作为癌症的潜在治疗靶点。在这篇综述中,我们简要概述了 SUMO 系统的基本概念,并总结了 SUMO 蛋白在癌细胞中的参与,以更好地理解 SUMO 在人类疾病中的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0cd/5843405/3094d4a9e8d7/IJO-52-04-1081-g02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0cd/5843405/c937774b5c07/IJO-52-04-1081-g00.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0cd/5843405/08daff0de4ad/IJO-52-04-1081-g01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0cd/5843405/3094d4a9e8d7/IJO-52-04-1081-g02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0cd/5843405/c937774b5c07/IJO-52-04-1081-g00.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0cd/5843405/08daff0de4ad/IJO-52-04-1081-g01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f0cd/5843405/3094d4a9e8d7/IJO-52-04-1081-g02.jpg

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Tumour Biol. 2017 Mar;39(3):1010428317694543. doi: 10.1177/1010428317694543.
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Silencing Trim59 inhibits invasion/migration and epithelial-to-mesenchymal transition via TGF-β/Smad2/3 signaling pathway in bladder cancer cells.
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