Ubiquitylation in innate and adaptive immunity

被引：507

作者：

Bhoj, Vijay G. ^{[1
]}

Chen, Zhijian J. ^{[1
,2
]}

机构：

[1] Univ Texas SW Med Ctr Dallas, Dept Mol Biol, Dallas, TX 75390 USA

[2] Univ Texas SW Med Ctr Dallas, Howard Hughes Med Inst, Dallas, TX 75390 USA

来源：

NATURE | 2009年 / 458卷 / 7237期

基金：

美国国家卫生研究院;

关键词：

NF-KAPPA-B; E3 UBIQUITIN LIGASE; T-CELL-ACTIVATION; ALPHA-DEPENDENT APOPTOSIS; TUMOR-SUPPRESSOR CYLD; EDITING ENZYME A20; CBL-B; CONJUGATING ENZYME; POLYUBIQUITIN CHAINS; ANTIVIRAL RESPONSES;

D O I：

10.1038/nature07959

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Protein ubiquitylation has emerged as a key mechanism that regulates immune responses. Much like phosphorylation, ubiquitylation is a reversible covalent modification that regulates the stability, activity and localization of target proteins. As such, ubiquitylation regulates the development of the immune system and many phases of the immune response, including its initiation, propagation and termination. Recent work has shown that several ubiquitin ligases help to prevent the immune system from attacking self tissues. The dysfunction of several ubiquitin ligases has been linked to autoimmune diseases.

引用

页码：430 / 437

页数：8

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