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泛素酶在免疫反应调节中的作用

Ubiquitin enzymes in the regulation of immune responses.

作者信息

Ebner Petra, Versteeg Gijs A, Ikeda Fumiyo

机构信息

a IMBA , Vienna , Austria.

b MFPL , Vienna , Austria.

出版信息

Crit Rev Biochem Mol Biol. 2017 Aug;52(4):425-460. doi: 10.1080/10409238.2017.1325829. Epub 2017 May 19.

DOI:10.1080/10409238.2017.1325829
PMID:28524749
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5490640/
Abstract

Ubiquitination plays a central role in the regulation of various biological functions including immune responses. Ubiquitination is induced by a cascade of enzymatic reactions by E1 ubiquitin activating enzyme, E2 ubiquitin conjugating enzyme, and E3 ubiquitin ligase, and reversed by deubiquitinases. Depending on the enzymes, specific linkage types of ubiquitin chains are generated or hydrolyzed. Because different linkage types of ubiquitin chains control the fate of the substrate, understanding the regulatory mechanisms of ubiquitin enzymes is central. In this review, we highlight the most recent knowledge of ubiquitination in the immune signaling cascades including the T cell and B cell signaling cascades as well as the TNF signaling cascade regulated by various ubiquitin enzymes. Furthermore, we highlight the TRIM ubiquitin ligase family as one of the examples of critical E3 ubiquitin ligases in the regulation of immune responses.

摘要

泛素化在包括免疫反应在内的各种生物学功能的调节中起着核心作用。泛素化由E1泛素激活酶、E2泛素结合酶和E3泛素连接酶的一系列酶促反应诱导,并由去泛素化酶逆转。根据这些酶的不同,会产生或水解特定连接类型的泛素链。由于不同连接类型的泛素链控制着底物的命运,因此了解泛素酶的调节机制至关重要。在本综述中,我们重点介绍了泛素化在免疫信号级联反应中的最新知识,包括T细胞和B细胞信号级联反应以及由各种泛素酶调节的TNF信号级联反应。此外,我们重点介绍了TRIM泛素连接酶家族,作为免疫反应调节中关键E3泛素连接酶的例子之一。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/e940d0861670/ibmg_a_1325829_f0007_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/10b3662adb2e/ibmg_a_1325829_f0001_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/557d4e4f4f2f/ibmg_a_1325829_f0002_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/fd1130c64b91/ibmg_a_1325829_f0003_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/187ec59f7351/ibmg_a_1325829_f0004_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/f4e6d1bebfb4/ibmg_a_1325829_f0005_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/445cb5dcc173/ibmg_a_1325829_f0006_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/e940d0861670/ibmg_a_1325829_f0007_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/10b3662adb2e/ibmg_a_1325829_f0001_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/557d4e4f4f2f/ibmg_a_1325829_f0002_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/fd1130c64b91/ibmg_a_1325829_f0003_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/187ec59f7351/ibmg_a_1325829_f0004_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/f4e6d1bebfb4/ibmg_a_1325829_f0005_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/445cb5dcc173/ibmg_a_1325829_f0006_c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dac4/5490640/e940d0861670/ibmg_a_1325829_f0007_c.jpg

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