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E3泛素连接酶:类型、结构与功能

E3 ubiquitin ligases: styles, structures and functions.

作者信息

Yang Quan, Zhao Jinyao, Chen Dan, Wang Yang

机构信息

Second Affiliated Hospital, Institute of Cancer Stem Cell, Dalian Medical University, Dalian, 116044, China.

Department of Pathology, First Affiliated Hospital, Dalian Medical University, Dalian, 116044, China.

出版信息

Mol Biomed. 2021 Jul 30;2(1):23. doi: 10.1186/s43556-021-00043-2.

DOI:10.1186/s43556-021-00043-2
PMID:35006464
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8607428/
Abstract

E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2. E3 ubiquitin ligases play an essential role in catalyzing the ubiquitination process and transferring ubiquitin protein to attach the lysine site of targeted substrates. Importantly, ubiquitination modification is involved in almost all life activities of eukaryotes. Thus, E3 ligases might be involved in regulating various biological processes and cellular responses to stress signal associated with cancer development. Thanks to their multi-functions, E3 ligases can be a promising target of cancer therapy. A deeper understanding of the regulatory mechanisms of E3 ligases in tumorigenesis will help to find new prognostic markers and accelerate the growth of anticancer therapeutic approaches. In general, we mainly introduce the classifications of E3 ligases and their important roles in cancer progression and therapeutic functions.

摘要

E3泛素连接酶是一大类酶,它们与泛素激活酶E1和泛素结合酶E2一起参与三酶泛素化级联反应。E3泛素连接酶在催化泛素化过程以及转移泛素蛋白以附着到靶向底物的赖氨酸位点方面发挥着至关重要的作用。重要的是,泛素化修饰几乎涉及真核生物的所有生命活动。因此,E3连接酶可能参与调节各种生物学过程以及细胞对与癌症发展相关的应激信号的反应。由于其多功能性,E3连接酶可能成为癌症治疗的一个有前景的靶点。深入了解E3连接酶在肿瘤发生中的调控机制将有助于找到新的预后标志物并加速抗癌治疗方法的发展。总体而言,我们主要介绍E3连接酶的分类及其在癌症进展和治疗功能中的重要作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/78d5bac7277b/43556_2021_43_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/4e1de838e288/43556_2021_43_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/2854a1b4780d/43556_2021_43_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/a26d490f6469/43556_2021_43_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/4894255537ac/43556_2021_43_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/78d5bac7277b/43556_2021_43_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/4e1de838e288/43556_2021_43_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/2854a1b4780d/43556_2021_43_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/a26d490f6469/43556_2021_43_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/4894255537ac/43556_2021_43_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01ff/8607428/78d5bac7277b/43556_2021_43_Fig5_HTML.jpg

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